Journal articles: 'Formina2'

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Kaminski, Lucas A., Sebastián F. Sendoya, André V. L. Freitas, and Paulo S. Oliveira. "ECOLOGIA COMPORTAMENTAL NA INTERFACE FORMIGA-PLANTA-HERBÍVORO: INTERAÇÕES ENTRE FORMIGAS E LEPIDÓPTEROS." Oecologia Australis 13, no. 01 (March 2009): 27–44. http://dx.doi.org/10.4257/oeco.2009.1301.03.

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Silkworth, William T., Kristina L. Kunes, Grace C. Nickel, Martin L. Phillips, Margot E. Quinlan, and Christina L. Vizcarra. "The neuron-specific formin Delphilin nucleates nonmuscle actin but does not enhance elongation." Molecular Biology of the Cell 29, no. 5 (March 2018): 610–21. http://dx.doi.org/10.1091/mbc.e17-06-0363.

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The formin Delphilin binds the glutamate receptor, GluRδ2, in dendritic spines of Purkinje cells. Both proteins play a role in learning. To understand how Delphilin functions in neurons, we studied the actin assembly properties of this formin. Formins have a conserved formin homology 2 domain, which nucleates and associates with the fast-growing end of actin filaments, influencing filament growth together with the formin homology 1 (FH1) domain. The strength of nucleation and elongation varies widely across formins. Additionally, most formins have conserved domains that regulate actin assembly through an intramolecular interaction. Delphilin is distinct from other formins in several ways: its expression is limited to Purkinje cells, it lacks classical autoinhibitory domains, and its FH1 domain has minimal proline-rich sequence. We found that Delphilin is an actin nucleator that does not accelerate elongation, although it binds to the barbed end of filaments. In addition, Delphilin exhibits a preference for actin isoforms, nucleating nonmuscle actin but not muscle actin, which has not been described or systematically studied in other formins. Finally, Delphilin is the first formin studied that is not regulated by intramolecular interactions. We speculate how the activity we observe is consistent with its localization in the small dendritic spines.

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Vizcarra, Christina L., Batbileg Bor, and Margot E. Quinlan. "The Role of Formin Tails in Actin Nucleation, Processive Elongation, and Filament Bundling." Journal of Biological Chemistry 289, no. 44 (September 22, 2014): 30602–13. http://dx.doi.org/10.1074/jbc.m114.588368.

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Formins are multidomain proteins that assemble actin in a wide variety of biological processes. They both nucleate and remain processively associated with growing filaments, in some cases accelerating filament growth. The well conserved formin homology 1 and 2 domains were originally thought to be solely responsible for these activities. Recently a role in nucleation was identified for the Diaphanous autoinhibitory domain (DAD), which is C-terminal to the formin homology 2 domain. The C-terminal tail of the Drosophila formin Cappuccino (Capu) is conserved among FMN formins but distinct from other formins. It does not have a DAD domain. Nevertheless, we find that Capu-tail plays a role in filament nucleation similar to that described for mDia1 and other formins. Building on this, replacement of Capu-tail with DADs from other formins tunes nucleation activity. Capu-tail has low-affinity interactions with both actin monomers and filaments. Removal of the tail reduces actin filament binding and bundling. Furthermore, when the tail is removed, we find that processivity is compromised. Despite decreased processivity, the elongation rate of filaments is unchanged. Again, replacement of Capu-tail with DADs from other formins tunes the processive association with the barbed end, indicating that this is a general role for formin tails. Our data show a role for the Capu-tail domain in assembling the actin cytoskeleton, largely mediated by electrostatic interactions. Because of its multifunctionality, the formin tail is a candidate for regulation by other proteins during cytoskeletal rearrangements.

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Isogai, Tadamoto, and Metello Innocenti. "New nuclear and perinuclear functions of formins." Biochemical Society Transactions 44, no. 6 (December 2, 2016): 1701–8. http://dx.doi.org/10.1042/bst20160187.

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Formin family proteins (formins) represent an evolutionary conserved protein family encoded in the genome of a wide range of eukaryotes. Formins are hallmarked by a formin homology 1 (FH1) domain juxtaposed to an FH2 domain whereby they control actin and microtubule dynamics. Not surprisingly, formins are best known as key regulators of the cytoskeleton in a variety of morphogenetic processes. However, mounting evidence implicates several formins in the assembly and organization of actin within and around the nucleus. In addition, actin-independent roles for formins have recently been discovered. In this mini-review, we summarize these findings and highlight the novel nuclear and perinulcear functions of formins. In light of the emerging new biology of formins, we also discuss the fundamental principles governing the versatile activity and multimodal regulation of these proteins.

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Dong, Yuqing, David Pruyne, and Anthony Bretscher. "Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast." Journal of Cell Biology 161, no. 6 (June 16, 2003): 1081–92. http://dx.doi.org/10.1083/jcb.200212040.

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Formins are actin filament nucleators regulated by Rho-GTPases. In budding yeast, the formins Bni1p and Bnr1p direct the assembly of actin cables, which guide polarized secretion and growth. From the six yeast Rho proteins (Cdc42p and Rho1–5p), we have determined that four participate in the regulation of formin activity. We show that the essential function of Rho3p and Rho4p is to activate the formins Bni1p and Bnr1p, and that activated alleles of either formin are able to bypass the requirement for these Rho proteins. Through a separate signaling pathway, Rho1p is necessary for formin activation at elevated temperatures, acting through protein kinase C (Pkc1p), the major effector for Rho1p signaling to the actin cytoskeleton. Although Pkc1p also activates a MAPK pathway, this pathway does not function in formin activation. Formin-dependent cable assembly does not require Cdc42p, but in the absence of Cdc42p function, cable assembly is not properly organized during initiation of bud growth. These results show that formin function is under the control of three distinct, essential Rho signaling pathways.

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Sherer, Laura A., Mark E. Zweifel, and Naomi Courtemanche. "Dissection of two parallel pathways for formin-mediated actin filament elongation." Journal of Biological Chemistry 293, no. 46 (September 28, 2018): 17917–28. http://dx.doi.org/10.1074/jbc.ra118.004845.

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Formins direct the elongation of unbranched actin filaments that are incorporated into a diverse set of cytoskeletal structures. Elongation of formin-bound filaments occurs along two parallel pathways. The formin homology 2 (FH2) pathway allows actin monomers to bind directly to barbed ends bound by dimeric FH2 domains. The formin homology 1 (FH1) pathway involves transfer of profilin-bound actin to the barbed end from polyproline tracts located in the disordered FH1 domains. Here, we used a total internal reflection fluorescence (TIRF) microscopy-based fluorescence approach to determine the fraction of actin subunits incorporated via the FH1 and FH2 pathways during filament elongation mediated by two formins. We found that the fraction of filament elongation that occurs via each pathway directly depends on the efficiency of the other pathway, indicating that these two pathways compete with each other for subunit addition by formins. We conclude that this competition allows formins to compensate for changes in the efficiency of one pathway by adjusting the frequency of subunit addition via the other, thus increasing the overall robustness of formin-mediated actin polymerization.

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Kollárová, Eva, Anežka Baquero Forero, Lenka Stillerová, Sylva Přerostová, and Fatima Cvrčková. "Arabidopsis Class II Formins AtFH13 and AtFH14 Can Form Heterodimers but Exhibit Distinct Patterns of Cellular Localization." International Journal of Molecular Sciences 21, no. 1 (January 5, 2020): 348. http://dx.doi.org/10.3390/ijms21010348.

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Formins are evolutionarily conserved multi-domain proteins participating in the control of both actin and microtubule dynamics. Angiosperm formins form two evolutionarily distinct families, Class I and Class II, with class-specific domain layouts. The model plant Arabidopsis thaliana has 21 formin-encoding loci, including 10 Class II members. In this study, we analyze the subcellular localization of two A. thaliana Class II formins exhibiting typical domain organization, the so far uncharacterized formin AtFH13 (At5g58160) and its distant homolog AtFH14 (At1g31810), previously reported to bind microtubules. Fluorescent protein-tagged full length formins and their individual domains were transiently expressed in Nicotiana benthamiana leaves under the control of a constitutive promoter and their subcellular localization (including co-localization with cytoskeletal structures and the endoplasmic reticulum) was examined using confocal microscopy. While the two formins exhibit distinct and only partially overlapping localization patterns, they both associate with microtubules via the conserved formin homology 2 (FH2) domain and with the periphery of the endoplasmic reticulum, at least in part via the N-terminal PTEN (Phosphatase and Tensin)-like domain. Surprisingly, FH2 domains of AtFH13 and AtFH14 can form heterodimers in the yeast two-hybrid assay—a first case of potentially biologically relevant formin heterodimerization mediated solely by the FH2 domain.

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Bersee, H. E. N., S. Lindstedt, and A. Beukers. "C-4 DIAPHRAGM FORMING OF THERMOSET COMPOSITES(Session: Forming I)." Proceedings of the Asian Symposium on Materials and Processing 2006 (2006): 51. http://dx.doi.org/10.1299/jsmeasmp.2006.51.

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Zhang, Laining, Tetyana Smertenko, Deirdre Fahy, Nuria Koteyeva, Natalia Moroz, Anna Kuchařová, Dominik Novák, et al. "Analysis of formin functions during cytokinesis using specific inhibitor SMIFH2." Plant Physiology 186, no. 2 (February 23, 2021): 945–63. http://dx.doi.org/10.1093/plphys/kiab085.

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Abstract The phragmoplast separates daughter cells during cytokinesis by constructing the cell plate, which depends on interaction between cytoskeleton and membrane compartments. Proteins responsible for these interactions remain unknown, but formins can link cytoskeleton with membranes and several members of formin protein family localize to the cell plate. Progress in functional characterization of formins in cytokinesis is hindered by functional redundancies within the large formin gene family. We addressed this limitation by employing Small Molecular Inhibitor of Formin Homology 2 (SMIFH2), a small-molecule inhibitor of formins. Treatment of tobacco (Nicotiana tabacum) tissue culture cells with SMIFH2 perturbed localization of actin at the cell plate; slowed down both microtubule polymerization and phragmoplast expansion; diminished association of dynamin-related proteins with the cell plate independently of actin and microtubules; and caused cell plate swelling. Another impact of SMIFH2 was shortening of the END BINDING1b (EB1b) and EB1c comets on the growing microtubule plus ends in N. tabacum tissue culture cells and Arabidopsis thaliana cotyledon epidermis cells. The shape of the EB1 comets in the SMIFH2-treated cells resembled that of the knockdown mutant of plant Xenopus Microtubule-Associated protein of 215 kDa (XMAP215) homolog MICROTUBULE ORGANIZATION 1/GEMINI 1 (MOR1/GEM1). This outcome suggests that formins promote elongation of tubulin flares on the growing plus ends. Formins AtFH1 (A. thaliana Formin Homology 1) and AtFH8 can also interact with EB1. Besides cytokinesis, formins function in the mitotic spindle assembly and metaphase to anaphase transition. Our data suggest that during cytokinesis formins function in: (1) promoting microtubule polymerization; (2) nucleating F-actin at the cell plate; (3) retaining dynamin-related proteins at the cell plate; and (4) remodeling of the cell plate membrane.

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Gao, Lina, and Anthony Bretscher. "Polarized Growth in Budding Yeast in the Absence of a Localized Formin." Molecular Biology of the Cell 20, no. 10 (May 15, 2009): 2540–48. http://dx.doi.org/10.1091/mbc.e09-03-0194.

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Polarity is achieved partly through the localized assembly of the cytoskeleton. During growth in budding yeast, the bud cortex and neck localized formins Bni1p and Bnr1p nucleate and assemble actin cables that extend along the bud-mother axis, providing tracks for secretory vesicle delivery. Localized formins are believed to determine the location and polarity of cables, hence growth. However, yeast expressing the nonlocalized actin nucleating/assembly formin homology (FH) 1-FH2 domains of Bnr1p or Bni1p as the sole formin grow well. Although cables are significantly disorganized, analysis of directed transport of secretory vesicles is still biased toward the bud, reflecting a bias in correctly oriented cables, thereby permitting polarized growth. Myosin II, localized at the bud neck, contributes to polarized growth as a mutant unable to interact with F-actin further compromises growth in cells with an unlocalized formin but not with a localized formin. Our results show that multiple mechanisms contribute to cable orientation and polarized growth, with localized formins and myosin II being two major contributors.

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Otsu, Masaaki, Hikaru Fukugawa, and Kazuki Takashima. "C-1 LASER FORMING OF GLASS AND SILICON FOILS(Session: Forming I)." Proceedings of the Asian Symposium on Materials and Processing 2006 (2006): 48. http://dx.doi.org/10.1299/jsmeasmp.2006.48.

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Eskin, Julian A., Aneliya Rankova, Adam B. Johnston, Salvatore L. Alioto, and Bruce L. Goode. "Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo." Molecular Biology of the Cell 27, no. 5 (March 2016): 828–37. http://dx.doi.org/10.1091/mbc.e15-09-0639.

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Formins comprise a large family of proteins with diverse roles in remodeling the actin cytoskeleton. However, the spatiotemporal mechanisms used by cells to control formin activities are only beginning to be understood. Here we dissected Smy1, which has dual roles in regulating formins and myosin. Using mutagenesis, we identified specific sequences in Smy1 critical for its in vitro inhibitory effects on the FH2 domain of the formin Bnr1. By integrating smy1 alleles targeting those sequences, we genetically uncoupled Smy1’s functions in regulating formins and myosin. Quantitative imaging analysis further demonstrated that the ability of Smy1 to directly control Bnr1 activity is crucial in vivo for proper actin cable length, shape, and velocity and, in turn, efficient secretory vesicle transport. A Smy1-like sequence motif was also identified in a different Bnr1 regulator, Bud14, and found to be essential for Bud14 functions in regulating actin cable architecture and function in vivo. Together these observations reveal unanticipated mechanistic ties between two distinct formin regulators. Further, they emphasize the importance of tightly controlling formin activities in vivo to generate specialized geometries and dynamics of actin structures tailored to their physiological roles.

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Kidokoro-Kobayashi, Midori, Misako Iwakura, Nao Fujiwara-Tsujii, Shingo Fujiwara, Midori Sakura, Hironori Sakamoto, Seigo Higashi, Abraham Hefetz, and Mamiko Ozaki. "Chemical Discrimination and Aggressiveness via Cuticular Hydrocarbons in a Supercolony-Forming Ant, Formica yessensis." PLoS ONE 7, no. 10 (October 24, 2012): e46840. http://dx.doi.org/10.1371/journal.pone.0046840.

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Daou, Pascale, Salma Hasan, Dennis Breitsprecher, Emilie Baudelet, Luc Camoin, Stéphane Audebert, Bruce L. Goode, and Ali Badache. "Essential and nonredundant roles for Diaphanous formins in cortical microtubule capture and directed cell migration." Molecular Biology of the Cell 25, no. 5 (March 2014): 658–68. http://dx.doi.org/10.1091/mbc.e13-08-0482.

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Formins constitute a large family of proteins that regulate the dynamics and organization of both the actin and microtubule cytoskeletons. Previously we showed that the formin mDia1 helps tether microtubules at the cell cortex, acting downstream of the ErbB2 receptor tyrosine kinase. Here we further study the contributions of mDia1 and its two most closely related formins, mDia2 and mDia3, to cortical microtubule capture and ErbB2-dependent breast carcinoma cell migration. We find that depletion of each of these three formins strongly disrupts chemotaxis without significantly affecting actin-based structures. Further, all three formins are required for formation of cortical microtubules in a nonredundant manner, and formin proteins defective in actin polymerization remain active for microtubule capture. Using affinity purification and mass spectrometry analysis, we identify differential binding partners of the formin-homology domain 2 (FH2) of mDia1, mDia2, and mDia3, which may explain their nonredundant roles in microtubule capture. The FH2 domain of mDia1 specifically interacts with Rab6-interacting protein 2 (Rab6IP2). Further, mDia1 is required for cortical localization of Rab6IP2, and concomitant depletion of Rab6IP2 and IQGAP1 severely disrupts cortical capture of microtubules, demonstrating the coinvolvement of mDia1, IQGAP1, and Rab6IP2 in microtubule tethering at the leading edge.

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Chang, Shuwei, Zhanhong Ren, Chang Liu, Pingzhou Du, Jingbin Li, Zengyu Liu, Fengli Zhang, et al. "OsFH3 Encodes a Type II Formin Required for Rice Morphogenesis." International Journal of Molecular Sciences 22, no. 24 (December 9, 2021): 13250. http://dx.doi.org/10.3390/ijms222413250.

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The actin cytoskeleton is crucial for plant morphogenesis, and organization of actin filaments (AF) is dynamically regulated by actin-binding proteins. However, the roles of actin-binding proteins, particularly type II formins, in this process remain poorly understood in plants. Here, we report that a type II formin in rice, Oryza sativa formin homolog 3 (OsFH3), acts as a major player to modulate AF dynamics and contributes to rice morphogenesis. osfh3 mutants were semi-dwarf with reduced size of seeds and unchanged responses to light or gravity compared with mutants of osfh5, another type II formin in rice. osfh3 osfh5 mutants were dwarf with more severe developmental defectiveness. Recombinant OsFH3 could nucleate actin, promote AF bundling, and cap the barbed end of AF to prevent elongation and depolymerization, but in the absence of profilin, OsFH3 could inhibit AF elongation. Different from other reported type II formins, OsFH3 could bind, but not bundle, microtubules directly. Furthermore, its N-terminal phosphatase and tensin homolog domain played a key role in modulating OsFH3 localization at intersections of AF and punctate structures of microtubules, which differed from other reported plant formins. Our results, thus, provide insights into the biological function of type II formins in modulating plant morphology by acting on AF dynamics.

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Shi, Xuemeng, Daijiao Tang, Yifan Xing, Shuangshuang Zhao, Changyuan Fan, Jin Zhong, Yanqin Cui, Kun Shi, and Yaming Jiu. "Actin nucleator formins regulate the tension-buffering function of caveolin-1." Journal of Molecular Cell Biology 13, no. 12 (October 27, 2021): 876–88. http://dx.doi.org/10.1093/jmcb/mjab070.

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Abstract Both the mechanosensitive actin cytoskeleton and caveolae contribute to active processes such as cell migration, morphogenesis, and vesicular trafficking. Although distinct actin components are well studied, how they contribute to cytoplasmic caveolae, especially in the context of mechano-stress, has remained elusive. Here, we identify two actin-associated mobility stereotypes of caveolin-1 (CAV-1)-marked intracellular vesicles, which are characterized as ‘dwelling’ and ‘go and dwelling’. In order to exploit the reason for their distinct dynamics, elongated actin-associated formin functions are perturbed. We find drastically decreased density, increased clustering, and compromised motility of cytoplasmic CAV-1 vesicles resulting from lacking actin nucleator formins by both chemical treatment and RNA silencing of formin genes. Furthermore, hypo-osmosis-stimulated diminishing of CAV-1 is dramatically intensified upon blocking formins. The clustering of CAV-1 vesicles when cells are cultured on soft substrate is also aggravated under formin inhibition condition. Together, we reveal that actin-associated formins are essential for maintaining the dynamic organization of cytoplasmic CAV-1 and importantly its sensitivity upon mechanical challenge. We conclude that tension-controlled actin formins act as a safety valve dampening excessive tension on CAV-1 and safeguarding CAV-1 against mechanical damage.

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Mague, Joel T., Alaa A. M. Abdel-Aziz, Adel S. El-Azab, and Amer M. Alanazi. "1-Acetyl-5-methoxy-4-(phenylsulfanyl)imidazolidin-2-one." Acta Crystallographica Section E Structure Reports Online 70, no. 2 (January 15, 2014): o145—o146. http://dx.doi.org/10.1107/s1600536814000117.

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The title compound, C12H14N2O3S, crystallizes with two independent molecules (AandB) in the asymmetric unit. The five-membered imidazolidin-2-one rings in both molecules are twisted about the C—C bond. In the crystal, theAandBmolecules are associatedviapairs of N—H...O hydrogen bonds, formingA–Bdimers. These dimers are linkedviaC—H...S hydrogen bonds, forming double dimers, which are in turn linkedviaC—H...O hydrogen bonds forming two-dimensional networks lying parallel to (001). There are also C—H...π interactions present, which consolide the layers and link them, so forming a three-dimensional structure.

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Fedulova, Iryna Valentynivna, and Julia Anatoliivna Sagaydack. "FORMING COMPANY’S RISK APPETITE." SCIENTIFIC BULLETIN OF POLISSIA 1, no. 1(13) (2018): 47–53. http://dx.doi.org/10.25140/2410-9576-2018-1-1(13)-47-53.

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Fonseca, Carlos Roberto. "Amazonian ant–plant interactions and the nesting space limitation hypothesis." Journal of Tropical Ecology 15, no. 6 (November 1999): 807–25. http://dx.doi.org/10.1017/s0266467499001194.

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ABSTRACT: Throughout the tropics there are a few hundred ant species that nest exclusively inside myrmecophytes (i.e. ant-domatia bearing plants). For these ants, nesting space is an essential resource that must be shared among them, therefore opening the possibility for strong intraspecific and interspecific competition. Several ant–myrmecophyte systems from Central Amazonia were investigated to test the relevance and generality of the nesting space limitation hypothesis for plant-ants. Empirical patterns were drawn at four organizational levels: (a) individual level—ant species with small-bodied queens were the most frequent partners of myrmecophyte species offering small-sized domatia, while ants with large-bodied queens dominated host species with large-sized domatia, suggesting that host choice by inseminated queens and interspecific conflicts over host dominance seem to be influenced by space limitation; (b) colony level—in eight independent ant–myrmecophyte systems, ant colony size was positively correlated to the number of domatia provided by the host, and the mean occupancy level of the domatia by ants was 92%, suggesting that space can be limiting to colony growth; (c) population level—ant colony number and distribution was determined by the local availability and distribution of its plant partners; and (d) community level—across ant-myrmecophyte systems, the commonness of ant species were largely determined by the commonness of their specialized host partners. Within ant-myrmecophyte systems, rarity of ants seems to be defined by interspecific conflicts over host dominance. The ecological and evolutionary consequences of those patterns are discussed.RESUMO. Nos trópicos existem algumas poucas centenas de espécies de formigas que nidificam exclusivamente dentro de mirmecófitas (i.e. plantas possuidoras de domácias). Para estas formigas, o espaço de nidificação é um recurso essencial que precisa ser dividido entre elas, abrindo assim a possibilidade de competição intraespecífica e interespecífica forte. Diversos sistemas formiga-plantas da Amazônia Central foram investigados para se testar a relevância e generalidade da hipótese da limitação de sítios de nidificação para formigas associadas às mirmecófitas. Padrões empíricos foram gerados a quatro níveis organizacionais: (a) nível individual—espécies de formigas com rainhas de tamanho corpóreo reduzido foram os parceiros mais frequentes de espécies de mirmecófitas que oferecem domácias pequenas, enquanto que espécies de rainhas grandes dominam espécies de hospedeiros que oferecem domácias grandes, sugerindo que a escolha de hospedeiros por rainhas inseminadas e conflitos interespecíficos pela dominância do hospedeiro parecem ser influenciados por limitações de espaço; (b) nível da colônia—em oito sistemas formiga-plantas independentes, o tamanho da colônia das formigas foi positivamente correlacionado ao número de domácias oferecido pelo hospedeiro, e o nível médio de ocupação das domácias por formigas foi 92%, sugerindo que espaço pode estar limitando o crescimento das colônias; (c) nível da população—o número e a distribuição das colônias de formigas foi determinado pela disponibilidade local e distribuição dos parceiros vegetais; e (d) nível da comunidade—entre os sistemas formiga-plantas, formigas comuns e raras correspondem a aquelas especializadas respectivamente em espécies de mirmecófitas comuns e raras. Dentro de cada sistema formiga-planta, a raridade das formigas parece ser definida por conflitos interespecíficos sobre a dominância dos hospedeiros. As conseqüências ecológicas e evolutivas destes padrões são discutidas.

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Higashi, Tomohito, Rachel E. Stephenson, and Ann L. Miller. "Comprehensive analysis of formin localization in Xenopus epithelial cells." Molecular Biology of the Cell 30, no. 1 (January 2019): 82–95. http://dx.doi.org/10.1091/mbc.e18-02-0133.

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Reorganization of the actin cytoskeleton is crucial for cellular processes, including cytokinesis and cell–cell junction remodeling. Formins are conserved processive actin-polymerizing machines that regulate actin dynamics by nucleating, elongating, and bundling linear actin filaments. Because the formin family is large, with at least 15 members in vertebrates, there have not been any comprehensive studies examining formin localization and function within a common cell type. Here, we characterized the localization of all 15 formins in epithelial cells of Xenopus laevis gastrula-stage embryos. Dia1 and Dia2 localized to tight junctions, while Fhod1 and Fhod3 localized to adherens junctions. Only Dia3 strongly localized at the cytokinetic contractile ring. The Diaphanous inhibitory domain–dimerization domain (DID-DD) region of Dia1 was sufficient for Dia1 localization, and overexpression of a Dia1 DID-DD fragment competitively removed Dia1 and Dia2 from cell–cell junctions. In Dia1 DID-DD–overexpressing cells, Dia1 and Dia2 were mislocalized to the contractile ring, and cells exhibited increased cytokinesis failure. This work provides a comprehensive analysis of the localization of all 15 vertebrate formins in epithelial cells and suggests that misregulated formin localization results in epithelial cytokinesis failure.

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Courtemanche, Naomi, and Thomas D. Pollard. "Determinants of Formin Homology 1 (FH1) Domain Function in Actin Filament Elongation by Formins." Journal of Biological Chemistry 287, no. 10 (January 14, 2012): 7812–20. http://dx.doi.org/10.1074/jbc.m111.322958.

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Gonçalves, Michel Gonçalves de, Alci Enimar Loeck, and João Luís Osório Rosado. "Primeiro registro de Camponotus cingulatus Mayr, 1862 (Hymenoptera: Formicidae) para o estado do Rio Grande do Sul, Brasil." Arquivos do Instituto Biológico 81, no. 1 (March 2014): 68–70. http://dx.doi.org/10.1590/s1808-16572014000100012.

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Uma colônia de formigas Camponotus cingulatus foi coletada e identificada a partir de uma floricultura no município de Capão do Leão, consistindo no seu primeiro registro para o estado do Rio Grande do Sul, Brasil. Por apresentar grande densidade de infestação, além de associação com hemípteros sugadores de seiva e agressividade ao serem perturbadas, essas formigas reduziram as vendas e tornaram-se um incômodo para o proprietário. Dessa forma, este registro aponta para a necessidade de pesquisas sobre essa formiga no estado.

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Matos, Lilian Caroline Nunes de, Flavia Delgado Santana, and Fabricio Beggiato Baccaro. "Relações alométricas entre os tamanhos de sementes artificiais removidas e de formigas em um fragmento florestal na Amazônia Central." Boletim do Museu Paraense Emílio Goeldi - Ciências Naturais 15, no. 1 (May 28, 2020): 155–64. http://dx.doi.org/10.46357/bcnaturais.v15i1.283.

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As formigas são os principais dispersores invertebrados de sementes encontradas no solo. No entanto, ainda conhecemos pouco sobre a história natural das espécies de formigas e como elas poderiam atuar na dispersão de sementes. Em busca de padrões alométricos entre formigas e sementes, que poderiam ser extrapolados para outros locais e outras espécies, comparamos modelos de sementes artificiais com tamanhos diferentes e os relacionamos com algumas medidas de tamanho das formigas. As sementes artificiais foram oferecidas em seis transectos com dez pontos de observação instalados no campus da Universidade Federal do Amazonas, em Manaus. Foram registradas 20 espécies de formigas interagindo com as sementes artificiais. Formigas do gênero Ectatomma removeram uma quantidade maior de sementes, seguidas por Pheidole, Odontomachus e Pachycondyla. A maior distância percorrida foi de 5,10 m, em um evento de dispersão por E. brunneum Smith, 1858. Formigas menores de 2 mm não removeram nenhum dos modelos de sementes artificiais, mas consumiram o arilo artificial no local onde a semente foi oferecida. Nossos resultados reforçam que a qualidade da dispersão de sementes é dependente da identidade do parceiro (espécie de formiga), mas que formigas maiores removem mais sementes e a distâncias maiores

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Fujii, Isao. "Crystal structure of (S)-2-amino-2-methylsuccinic acid." Acta Crystallographica Section E Crystallographic Communications 71, no. 10 (September 12, 2015): o731—o732. http://dx.doi.org/10.1107/s2056989015016709.

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The title compound, C5H9NO4, crystallized as a zwitterion. There is an intramolecular N—H...O hydrogen bond involving thetrans-succinic acid and the ammonium group, forming anS(6) ring motif. In the crystal, molecules are linked by O—H...O hydrogen bonds, formingC(7) chains along thec-axis direction. The chains are linked by N—H...O and C—H...O hydrogen bonds, forming sheets parallel to thebcplane. Further N—H...O hydrogen bonds link the sheets to form a three-dimensional framework.

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Pereira, Rogério dos Santos, and Mariko Ueno. "Formigas como veiculadoras de microrganismos em ambiente hospitalar." Revista da Sociedade Brasileira de Medicina Tropical 41, no. 5 (October 2008): 492–95. http://dx.doi.org/10.1590/s0037-86822008000500011.

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Existe preocupação sobre as reais possibilidades de agravos à saúde pública que possam ser causados pela veiculação de agentes patogênicos através de formigas urbanas. O presente trabalho teve por objetivo isolar e identificar os microrganismos associados às formigas em ambiente hospitalar. Foram coletadas 125 formigas, da mesma espécie, em diferentes unidades de um Hospital Universitário. Cada formiga foi coletada com swab embebido em solução fisiológica e transferida para um tubo com caldo Brain Heart Infusion e incubados 35ºC por 24 horas. A partir de cada tubo, com crescimento, foram realizadas inoculações, em meios específicos, para isolamento dos microrganismos. As formigas apresentaram alta capacidade de veiculação de grupos de microrganismos, sendo que 63,5% das cepas eram bacilos Gram positivos produtores de esporos, 6,3% eram bacilos Gram negativos, cocos Gram positivos corresponderam a 23,1% das cepas, 6,7% eram fungos filamentosos e 0,5% eram leveduras. Desta forma, pode-se inferir que as formigas podem ser um dos responsáveis pela disseminação de microrganismos em ambientes hospitalares.

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Rana, Manish K., Francesca M. Aloisio, Changhoon Choi, and Diane L. Barber. "Formin-dependent TGF-β signaling for epithelial to mesenchymal transition." Molecular Biology of the Cell 29, no. 12 (June 15, 2018): 1465–75. http://dx.doi.org/10.1091/mbc.e17-05-0325.

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The role of distinct actin filament architectures in epithelial plasticity remains incompletely understood. We therefore determined roles for formins and the Arp2/3 complex, which are actin nucleators generating unbranched and branched actin filaments, respectively, in the process of epithelial to mesenchymal transition (EMT). In clonal lung, mammary, and renal epithelial cells, the formin activity inhibitor SMIFH2 but not the Arp2/3 complex activity inhibitor CK666 blocked EMT induced by TGF-β. SMIFH2 prevented the proximal signal of increased Smad2 phosphorylation and hence also blocked downstream EMT markers, including actin filament remodeling, decreased expression of the adherens junction protein E-cadherin, and increased expression of the matrix protein fibronectin and the transcription factor Snail. The short hairpin RNA silencing of formins DIAPH1 and DIAPH3 but not other formins phenocopied SMIFH2 effects and inhibited Smad2 phosphorylation and changes in Snail and cadherin expression. Formin activity was not necessary for the cell surface expression or dimerization of TGF-β receptors, or for nuclear translocation of TAZ, a transcription cofactor in Hippo signaling also regulated by TGF-β. Our findings reveal a previously unrecognized role for formin-dependent actin architectures in proximal TGF-β signaling that is necessary for Smad2 phosphorylation but not for cross-talk to TAZ.

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Sodamuk, Sawad, Vichit Buakeaw, Suparerk Sirivadin, and Suwat Jirathearanat. "C-6 Formability Prediction of The Automotive Parts Using Forming Limit Diagrams(Session: Forming II)." Proceedings of the Asian Symposium on Materials and Processing 2006 (2006): 53. http://dx.doi.org/10.1299/jsmeasmp.2006.53.

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Higgs, Henry N., and Kevin J. Peterson. "Phylogenetic Analysis of the Formin Homology 2 Domain." Molecular Biology of the Cell 16, no. 1 (January 2005): 1–13. http://dx.doi.org/10.1091/mbc.e04-07-0565.

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Formin proteins are key regulators of eukaryotic actin filament assembly and elongation, and many species possess multiple formin isoforms. A nomenclature system based on fundamental features would be desirable, to aid the rapid identification and characterization of novel formins. In this article, we attempt to systematize the formin family by performing phylogenetic analyses of the formin homology 2 (FH2) domain, an independently folding region common to all formins, which alone can influence actin dynamics. Through database searches, we identify 101 FH2 domains from 26 eukaryotic species, including 15 in mice. Sequence alignments reveal a highly conserved yeast-specific insert in the “knob loop” region of the FH2 domain, with unknown functional consequences. Phylogenetic analysis using minimum evolution (ME), maximum parsimony (MP), and maximum likelihood (ML) algorithms strongly supports the existence of seven metazoan groups. Yeast FH2 domains segregate from all other eukaryotes, including metazoans, other fungi, plants, and protists. Sequence comparisons of non-FH2 regions support relationships between three metazoan groups (Dia, DAAM, and FRL) and examine previously identified coiled-coil and Diaphanous auto-regulatory domain sequences. This analysis allows for a formin nomenclature system based on sequence relationships, as well as suggesting strategies for the determination of biochemical and cellular activities of these proteins.

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Cvrčková, Fatima. "Formins: Emerging Players in the Dynamic Plant Cell Cortex." Scientifica 2012 (2012): 1–14. http://dx.doi.org/10.6064/2012/712605.

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Formins (FH2 proteins) are an evolutionarily conserved family of eukaryotic proteins, sharing the common FH2 domain. While they have been, until recently, understood mainly as actin nucleators, formins are also engaged in various additional aspects of cytoskeletal organization and signaling, including, but not limited to, the crosstalk between the actin and microtubule networks. A surprising diversity of domain organizations has been discovered among the FH2 proteins, and specific domain setups have been found in plants. Seed plants have two clades of formins, one of them (Class I) containing mostly transmembrane proteins, while members of the other one (Class II) may be anchored to membranes via a putative membrane-binding domain related to the PTEN antioncogene. Thus, plant formins present good candidates for possible mediators of coordination of the cortical actin and microtubule cytoskeletons, as well as their attachment to the plasma membrane, that is, aspects of cell cortex organization likely to be important for cell and tissue morphogenesis. Although experimental studies of plant formin function are hampered by the large number of formin genes and their functional redundancy, recent experimental work has already resulted in some remarkable insights into the function of FH2 proteins in plants.

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Garabedian, Mikael V., Tatiana Stanishneva-Konovalova, Chenyu Lou, Thomas J. Rands, Luther W. Pollard, Olga S. Sokolova, and Bruce L. Goode. "Integrated control of formin-mediated actin assembly by a stationary inhibitor and a mobile activator." Journal of Cell Biology 217, no. 10 (August 3, 2018): 3512–30. http://dx.doi.org/10.1083/jcb.201803164.

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Formins are essential actin assembly factors whose activities are controlled by a diverse array of binding partners. Until now, most formin ligands have been studied on an individual basis, leaving open the question of how multiple inputs are integrated to regulate formins in vivo. Here, we show that the F-BAR domain of Saccharomyces cerevisiae Hof1 interacts with the FH2 domain of the formin Bnr1 and blocks actin nucleation. Electron microscopy of the Hof1–Bnr1 complex reveals a novel dumbbell-shaped structure, with the tips of the F-BAR holding two FH2 dimers apart. Deletion of Hof1’s F-BAR domain in vivo results in disorganized actin cables and secretory defects. The formin-binding protein Bud6 strongly alleviates Hof1 inhibition in vitro, and bud6Δ suppresses hof1Δ defects in vivo. Whereas Hof1 stably resides at the bud neck, we show that Bud6 is delivered to the neck on secretory vesicles. We propose that Hof1 and Bud6 functions are intertwined as a stationary inhibitor and a mobile activator, respectively.

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Svatoš, M. "Selected trends forming European agriculture." Agricultural Economics (Zemědělská ekonomika) 54, No. 3 (March 31, 2008): 93–101. http://dx.doi.org/10.17221/238-agricecon.

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The dynamics and forming of European agriculture are determined by many considerably heterogenous and complicated processes and trends which influence mutually and moreover they work in a different way in developed and developing countries. An attention will be paid to basic global trends, the role of the Common Agricultural Policy, the influence of agrarian markets, the promotion of multifunctional agriculture etc.

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Gaillard, Jeremie, Vinay Ramabhadran, Emmanuelle Neumanne, Pinar Gurel, Laurent Blanchoin, Marylin Vantard, and Henry N. Higgs. "Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules." Molecular Biology of the Cell 22, no. 23 (December 2011): 4575–87. http://dx.doi.org/10.1091/mbc.e11-07-0616.

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A number of cellular processes use both microtubules and actin filaments, but the molecular machinery linking these two cytoskeletal elements remains to be elucidated in detail. Formins are actin-binding proteins that have multiple effects on actin dynamics, and one formin, mDia2, has been shown to bind and stabilize microtubules through its formin homology 2 (FH2) domain. Here we show that three formins, INF2, mDia1, and mDia2, display important differences in their interactions with microtubules and actin. Constructs containing FH1, FH2, and C-terminal domains of all three formins bind microtubules with high affinity (Kd < 100 nM). However, only mDia2 binds microtubules at 1:1 stoichiometry, with INF2 and mDia1 showing saturating binding at approximately 1:3 (formin dimer:tubulin dimer). INF2-FH1FH2C is a potent microtubule-bundling protein, an effect that results in a large reduction in catastrophe rate. In contrast, neither mDia1 nor mDia2 is a potent microtubule bundler. The C-termini of mDia2 and INF2 have different functions in microtubule interaction, with mDia2's C-terminus required for high-affinity binding and INF2's C-terminus required for bundling. mDia2's C-terminus directly binds microtubules with submicromolar affinity. These formins also differ in their abilities to bind actin and microtubules simultaneously. Microtubules strongly inhibit actin polymerization by mDia2, whereas they moderately inhibit mDia1 and have no effect on INF2. Conversely, actin monomers inhibit microtubule binding/bundling by INF2 but do not affect mDia1 or mDia2. These differences in interactions with microtubules and actin suggest differential function in cellular processes requiring both cytoskeletal elements.

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Chen, Hsin, Chun-Chen Kuo, Hui Kang, Audrey S. Howell, Trevin R. Zyla, Michelle Jin, and Daniel J. Lew. "Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p." Molecular Biology of the Cell 23, no. 19 (October 2012): 3814–26. http://dx.doi.org/10.1091/mbc.e12-05-0400.

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Actin filaments are dynamically reorganized to accommodate ever-changing cellular needs for intracellular transport, morphogenesis, and migration. Formins, a major family of actin nucleators, are believed to function as direct effectors of Rho GTPases, such as the polarity regulator Cdc42p. However, the presence of extensive redundancy has made it difficult to assess the in vivo significance of the low-affinity Rho GTPase–formin interaction and specifically whether Cdc42p polarizes the actin cytoskeleton via direct formin binding. Here we exploit a synthetically rewired budding yeast strain to eliminate the redundancy, making regulation of the formin Bni1p by Cdc42p essential for viability. Surprisingly, we find that direct Cdc42p–Bni1p interaction is dispensable for Bni1p regulation. Alternative paths linking Cdc42p and Bni1p via “polarisome” components Spa2p and Bud6p are also collectively dispensable. We identify a novel regulatory input to Bni1p acting through the Cdc42p effector, Gic2p. This pathway is sufficient to localize Bni1p to the sites of Cdc42p action and promotes a polarized actin organization in both rewired and wild-type contexts. We suggest that an indirect mechanism linking Rho GTPases and formins via Rho effectors may provide finer spatiotemporal control for the formin-nucleated actin cytoskeleton.

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Oulehlovï¿½, Denisa, Eva Kollï¿½rovï¿½, Petra Cifrovï¿½, Přemysl Pejchar, Viktor Žï¿½rskï¿½, and Fatima Cvrčkovï¿½. "Arabidopsis Class I Formin FH1 Relocates between Membrane Compartments during Root Cell Ontogeny and Associates with Plasmodesmata." Plant and Cell Physiology 60, no. 8 (May 28, 2019): 1855–70. http://dx.doi.org/10.1093/pcp/pcz102.

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Abstract Formins are evolutionarily conserved eukaryotic proteins engaged in actin nucleation and other aspects of cytoskeletal organization. Angiosperms have two formin clades with multiple paralogs; typical plant Class I formins are integral membrane proteins that can anchor cytoskeletal structures to membranes. For the main Arabidopsis housekeeping Class I formin, FH1 (At3g25500), plasmalemma localization was documented in heterologous expression and overexpression studies. We previously showed that loss of FH1 function increases cotyledon epidermal pavement cell shape complexity via modification of actin and microtubule organization and dynamics. Here, we employ transgenic Arabidopsis expressing green fluorescent protein-tagged FH1 (FH1-GFP) from its native promoter to investigate in vivo behavior of this formin using advanced microscopy techniques. The fusion protein is functional, since its expression complements the fh1 loss-of-function mutant phenotype. Accidental overexpression of FH1-GFP results in a decrease in trichome branch number, while fh1 mutation has the opposite effect, indicating a general role of this formin in controlling cell shape complexity. Consistent with previous reports, FH1-GFP associates with membranes. However, the protein exhibits surprising actin- and secretory pathway-dependent dynamic localization and relocates between cellular endomembranes and the plasmalemma during cell division and differentiation in root tissues, with transient tonoplast localization at the transition/elongation zones border. FH1-GFP also accumulates in actin-rich regions of cortical cytoplasm and associates with plasmodesmata in both the cotyledon epidermis and root tissues. Together with previous reports from metazoan systems, this suggests that formins might have a shared (ancestral or convergent) role at cell–cell junctions.

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Upton, N. P. D. "Asynchronous male and female life cycles in the sexually dimorphic, harem-forming isopodParagnathia formica(Crustacea: Isopoda)." Journal of Zoology 212, no. 4 (August 1987): 677–90. http://dx.doi.org/10.1111/j.1469-7998.1987.tb05964.x.

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Sun, H., J. S. Schlondorff, E. J. Brown, H. N. Higgs, and M. R. Pollak. "Rho activation of mDia formins is modulated by an interaction with inverted formin 2 (INF2)." Proceedings of the National Academy of Sciences 108, no. 7 (January 28, 2011): 2933–38. http://dx.doi.org/10.1073/pnas.1017010108.

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Michelot, Alphée, Christophe Guérin, Shanjin Huang, Mathieu Ingouff, Stéphane Richard, Natalia Rodiuc, Christopher J. Staiger, and Laurent Blanchoin. "The Formin Homology 1 Domain Modulates the Actin Nucleation and Bundling Activity of Arabidopsis FORMIN1." Plant Cell 17, no. 8 (July 1, 2005): 2296–313. http://dx.doi.org/10.1105/tpc.105.030908.

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Bor, Batbileg, Christina L. Vizcarra, Martin L. Phillips, and Margot E. Quinlan. "Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains." Molecular Biology of the Cell 23, no. 19 (October 2012): 3801–13. http://dx.doi.org/10.1091/mbc.e12-04-0288.

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Formins are a conserved family of proteins known to enhance actin polymerization. Most formins are regulated by an intramolecular interaction. The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. We report here that Capu is, in fact, autoinhibited. The N-terminal half of Capu (Capu-NT) potently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal half of Capu (Capu-CT). Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to the N-termini of other formins. These data, combined with those from circular dichroism, suggest, however, that it is structurally distinct from previously described formin inhibitory domains. Finally, we find that Capu-NT binds to a site within Capu-CT that overlaps with the Spire-binding site, the Capu-tail. We propose models for the interaction between Spire and Capu in light of the fact that Capu can be regulated by autoinhibition.

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Graziano, Brian R., Hoi-Ying E. Yu, Salvatore L. Alioto, Julian A. Eskin, Casey A. Ydenberg, David P. Waterman, Mikael Garabedian, and Bruce L. Goode. "The F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth." Molecular Biology of the Cell 25, no. 11 (June 2014): 1730–43. http://dx.doi.org/10.1091/mbc.e14-03-0850.

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Asymmetric cell growth and division rely on polarized actin cytoskeleton remodeling events, the regulation of which is poorly understood. In budding yeast, formins stimulate the assembly of an organized network of actin cables that direct polarized secretion. Here we show that the Fer/Cip4 homology–Bin amphiphysin Rvs protein Hof1, which has known roles in cytokinesis, also functions during polarized growth by directly controlling the activities of the formin Bnr1. A mutant lacking the C-terminal half of Hof1 displays misoriented and architecturally altered cables, along with impaired secretory vesicle traffic. In vitro, Hof1 inhibits the actin nucleation and elongation activities of Bnr1 without displacing the formin from filament ends. These effects depend on the Src homology 3 domain of Hof1, the formin homology 1 (FH1) domain of Bnr1, and Hof1 dimerization, suggesting a mechanism by which Hof1 “restrains” the otherwise flexible FH1-FH2 apparatus. In vivo, loss of inhibition does not alter actin levels in cables but, instead, cable shape and functionality. Thus Hof1 tunes formins to sculpt the actin cable network.

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Yartsev, Yegor, Vitaliy Palchikov, Alexandr Gaponov, and Svitlana Shishkina. "Crystal structure of 5-chloro-N1-(5-phenyl-1H-pyrazol-3-yl)benzene-1,2-diamine." Acta Crystallographica Section E Crystallographic Communications 73, no. 6 (May 26, 2017): 876–79. http://dx.doi.org/10.1107/s2056989017007381.

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The title compound, C15H13ClN4, crystallizes with two independent molecules (AandB) in the asymmetric unit, which are far from planar as a result of steric repulsion between the rings. The benzene and phenyl rings are inclined to the central pyrazole ring by 46.64 (10) and 17.87 (10)° in moleculeA, and by 40.02 (10) and 14.18 (10)° in moleculeB. The aromatic rings are inclined to one another by 58.77 (9)° in moleculeA, and 36.95 (8)° in moleculeB. In the crystal, theAandBmolecules are linked by two pairs of N—H...N hydrogen bonds formingA–Bdimers. These are further linked by a fifth N—H...N hydrogen bond, forming tetramer-like units that stack along thea-axis direction, forming columns, which are in turn linked by C—H...π interactions, forming layers parallel to theacplane.

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41

Gómez, D., A. Alegría, and J. Colmenero. "Relajación secundaria en sistemas formadores de vidrios." Boletín de la Sociedad Española de Cerámica y Vidrio 39, no. 3 (June 30, 2000): 371–73. http://dx.doi.org/10.3989/cyv.2000.v39.i3.861.

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Moreno, R. "Tendencias en el conformado de suspensiones cerámicas." Boletín de la Sociedad Española de Cerámica y Vidrio 39, no. 5 (October 30, 2000): 601–8. http://dx.doi.org/10.3989/cyv.2000.v39.i5.776.

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NAKAMURA, Toshihiko, Hideki AOYAMA, Naohisa MATSUSHITA, and Akihiko USHIMARU. "3298 Sheet Material Forming without Dies." Proceedings of International Conference on Leading Edge Manufacturing in 21st century : LEM21 2011.6 (2011): _3298–1_—_3298–4_. http://dx.doi.org/10.1299/jsmelem.2011.6._3298-1_.

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Machynia, Zbigniew, Grzegorz Skrabalak, Andrzej Stwora, and Maria Zybura. "Unconventional methods for forming implanto-distractors." Mechanik, no. 5-6 (May 2016): 542–43. http://dx.doi.org/10.17814/mechanik.2016.5-6.77.

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Abdupattoev, Mukhammadtokhir Tojimamatovich. "Unusual Connections As Forming Literary Text." American Journal of Social Science and Education Innovations 03, no. 02 (February 27, 2021): 177–82. http://dx.doi.org/10.37547/tajssei/volume03issue02-28.

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This article examines the role of the unusual connection in the formation of the literary text, which is a type of unusual connection in the Uzbek language. It has also been analyzed using examples that this tool is also a means of emotional expression in a literary text.

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Branson, Mark Lau. "FORMING CHURCH, FORMING MISSION." International Review of Mission 92, no. 365 (April 2003): 153–68. http://dx.doi.org/10.1111/j.1758-6631.2003.tb00391.x.

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Louie, Arnold, Brian D. VanScoy, David L. Brown, Robert W. Kulawy, Henry S. Heine, and George L. Drusano. "Impact of Spores on the Comparative Efficacies of Five Antibiotics for Treatment of Bacillus anthracis in anIn VitroHollow Fiber Pharmacodynamic Model." Antimicrobial Agents and Chemotherapy 56, no. 3 (December 12, 2011): 1229–39. http://dx.doi.org/10.1128/aac.01109-10.

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ABSTRACTBacillus anthracis, the bacterium that causes anthrax, is an agent of bioterrorism. The most effective antimicrobial therapy forB. anthracisinfections is unknown. Anin vitropharmacodynamic model ofB. anthraciswas used to compare the efficacies of simulated clinically prescribed regimens of moxifloxacin, linezolid, and meropenem with the “gold standards,” doxycycline and ciprofloxacin. Treatment outcomes for isogenic spore-forming and non-spore-forming strains ofB. anthraciswere compared. Against spore-formingB. anthracis, ciprofloxacin, moxifloxacin, linezolid, and meropenem reduced theB. anthracispopulation by 4 log10CFU/ml over 10 days. Doxycycline reduced the population of thisB. anthracisstrain by 5 log10CFU/ml (analysis of variance [ANOVA]P= 0.01 versus other drugs). Against an isogenic non-spore-forming strain, meropenem killed the vegetativeB. anthracisthe fastest, followed by moxifloxacin and ciprofloxacin and then doxycycline. Linezolid offered the lowest bacterial kill rate. Heat shock studies using the spore-producingB. anthracisstrain showed that with moxifloxacin, ciprofloxacin, and meropenem therapies the total population was mostly spores, while the population was primarily vegetative bacteria with linezolid and doxycycline therapies. Spores have a profound impact on the rate and extent of killing ofB. anthracis. Against spore-formingB. anthracis, the five antibiotics killed the total (spore and vegetative) bacterial population at similar rates (within 1 log10CFU/ml of each other). However, bactericidal antibiotics killed vegetativeB. anthracisfaster than bacteriostatic drugs. Since only vegetative-phaseB. anthracisproduces the toxins that may kill the infected host, the rate and mechanism of killing of an antibiotic may determine its overallin vivoefficacy. Further studies are needed to examine this important observation.

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Thiruvalluvar, A., M. Sridharan, K. J. Rajendra Prasad, and M. Zeller. "Crystal structure of (E)-2-(furan-2-ylmethylidene)-2,3,4,9-tetrahydro-1H-carbazol-1-one." Acta Crystallographica Section E Crystallographic Communications 74, no. 1 (January 1, 2018): 59–61. http://dx.doi.org/10.1107/s2056989017017972.

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The title compound, C17H13NO2, crystallizes with two conformationally very similar independent molecules (AandB) in the asymmetric unit. In the crystal, the individual molecules are linked by pairs of N—H...O hydrogen bonds formingA–AandB–Binversion dimers, withR22(10) rings. They stack alternately up thea-axis direction and are linked by C—H...π interactions, forming sheets parallel to theabplane.

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Harris, Elizabeth S., Fang Li, and Henry N. Higgs. "The Mouse Formin, FRLα, Slows Actin Filament Barbed End Elongation, Competes with Capping Protein, Accelerates Polymerization from Monomers, and Severs Filaments." Journal of Biological Chemistry 279, no. 19 (February 29, 2004): 20076–87. http://dx.doi.org/10.1074/jbc.m312718200.

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Formins are a conserved class of proteins expressed in all eukaryotes, with known roles in generating cellular actin-based structures. The mammalian formin, FRLα, is enriched in hematopoietic cells and tissues, but its biochemical properties have not been characterized. We show that a construct composed of the C-terminal half of FRLα (FRLα-C) is a dimer and has multiple effects on muscle actin, including tight binding to actin filament sides, partial inhibition of barbed end elongation, inhibition of barbed end binding by capping protein, acceleration of polymerization from monomers, and actin filament severing. These multiple activities can be explained by a model in which FRLα-C binds filament sides but prefers the topology of sides at the barbed end (end-sides) to those within the filament. This preference allows FRLα-C to nucleate new filaments by side stabilization of dimers, processively advance with the elongating barbed end, block interaction between C-terminal tentacles of capping protein and filament end-sides, and sever filaments by preventing subunit re-association as filaments bend. Another formin, mDia1, does not reduce the barbed end elongation rate but does block capping protein, further supporting an end-side binding model for formins. Profilin partially relieves barbed end elongation inhibition by FRLα-C. When non-muscle actin is used, FRLα-C's effects are largely similar. FRLα-C's ability to sever filaments is the first such activity reported for any formin. Because we find that mDia1-C does not sever efficiently, severing may not be a property of all formins.

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Majumder, Shubhra, and Anuradha Lohia. "Entamoeba histolytica Encodes Unique Formins, a Subset of Which Regulates DNA Content and Cell Division." Infection and Immunity 76, no. 6 (March 17, 2008): 2368–78. http://dx.doi.org/10.1128/iai.01449-07.

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ABSTRACT The formin family of proteins mediates dynamic changes in actin assembly in eukaryotes, and therefore it is important to understand the function of these proteins in Entamoeba histolytica, where actin forms the major cytoskeletal network. In this study we have identified the formin homologs encoded in the E. histolytica genome based on sequence analysis. Using multiple tools, we have analyzed the primary sequences of the eight E. histolytica formins and discovered three subsets: (i) E. histolytica formin-1 to -3 (Ehformin-1 to -3), (ii) Ehformin-4, and (iii) Ehformin-5 to -8. Two of these subsets (Ehformin-1 to -3 and Ehformin-4) showed significant sequence differences from their closest homologs, while Ehformin-5 to -8 were unique among all known formins. Since Ehformin-1 to -3 showed important sequence differences from Diaphanous-related formins (DRFs), we have studied the functions of Ehformin-1 and -2 in E. histolytica transformants. Like other DRFs, Ehformin-1 and -2 associated with F-actin in response to serum factors, in pseudopodia, in pinocytic and phagocytic vesicles, and at cell division sites. Ehformin-1 and -2 also localized with the microtubular assembly in the nucleus, indicating their involvement in genome segregation. While increased expression of Ehformin-1 and -2 did not affect phagocytosis or motility, it clearly showed an increase in the number of binucleated cells, the number of nuclei in multinucleated cells, and the average DNA content of each nucleus, suggesting that these proteins regulate both mitosis and cytokinesis in E. histolytica.

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Journal articles on the topic 'Formina2'

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