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Journal articles on the topic 'Actin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Roberts, Thomas M., and Murray Stewart. "Acting like Actin." Journal of Cell Biology 149, no. 1 (2000): 7–12. http://dx.doi.org/10.1083/jcb.149.1.7.

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2

Vinson, V. "Acting Like Actin." Science 330, no. 6009 (2010): 1289. http://dx.doi.org/10.1126/science.330.6009.1289-b.

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3

Marx, Vivien. "Actin in action." Nature Methods 20, no. 2 (2023): 178–82. http://dx.doi.org/10.1038/s41592-022-01762-2.

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4

Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120-4133.1988.

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The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions th

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5

Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120.

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The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions th

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6

P, RAGHAVENDRA K., RAKESH KUMAR, JOY DAS, et al. "Quantitative real-time PCR based evaluation and validation of reference genes in Gossypium arboreum." Indian Journal of Agricultural Sciences 90, no. 1 (2020): 40–47. http://dx.doi.org/10.56093/ijas.v90i1.98527.

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Estimation of gene expression levels plays a crucial role in understanding the function of the target gene(s). Intersample variance in gene expression can be more precisely measured if transcripts levels are accurately normalized. Normalization is pre-requisite step prior to the determination of candidate gene expression by qPCR. In this study conducted at ICAR-Central Institute for Cotton Research, Nagpur during 2015–16, six candidate reference genes, viz. actin4 (ACT4), actin7(ACT7), RNA Helicase (RNAH), Serine/threonine-protein phosphatase PP2A-1(PP2A1), ubiquitin7 (UBQ7) and α tubulin (αTU

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7

WINDER, Steven J., Thomas JESS, and Kathryn R. AYSCOUGH. "SCP1 encodes an actin-bundling protein in yeast." Biochemical Journal 375, no. 2 (2003): 287–95. http://dx.doi.org/10.1042/bj20030796.

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The association of F-actin (filamentous actin) with a large number of binding proteins is essential for cellular function. Actin-binding proteins control the dynamics of actin filaments, nucleate new filaments and facilitate formation of higher-order structures such as actin bundles. The yeast gene SCP1 encodes a small protein with significant homology to mammalian SM22/transgelin. We have investigated the role of Scp1p in budding yeast to probe the fundamental role of this family of proteins. Here, we demonstrate that Scp1p binds to F-actin and induces the formation of tight F-actin bundles i

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8

Hurtley, Stella M. "Parasite actin in action." Science 366, no. 6465 (2019): 584.6–585. http://dx.doi.org/10.1126/science.366.6465.584-f.

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9

Hurtley, S. M. "Nuclear Actin in Action." Science Signaling 6, no. 276 (2013): ec116-ec116. http://dx.doi.org/10.1126/scisignal.2004335.

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10

Geitmann, Anja. "Actuators Acting without Actin." Cell 166, no. 1 (2016): 15–17. http://dx.doi.org/10.1016/j.cell.2016.06.030.

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11

Kuběnová, Lenka, Tomáš Takáč, Jozef Šamaj, and Miroslav Ovečka. "Single Amino Acid Exchange in ACTIN2 Confers Increased Tolerance to Oxidative Stress in Arabidopsis der1–3 Mutant." International Journal of Molecular Sciences 22, no. 4 (2021): 1879. http://dx.doi.org/10.3390/ijms22041879.

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Single-point mutation in the ACTIN2 gene of the der1–3 mutant revealed that ACTIN2 is an essential actin isovariant required for root hair tip growth, and leads to shorter, thinner and more randomly oriented actin filaments in comparison to the wild-type C24 genotype. The actin cytoskeleton has been linked to plant defense against oxidative stress, but it is not clear how altered structural organization and dynamics of actin filaments may help plants to cope with oxidative stress. In this study, we characterized root growth, plant biomass, actin organization and antioxidant activity of the der

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12

Huang, Dichun. "Young and Senescent Cells: Distinct Nuclear F-actin Patterns Upon Latrunculin B Induction." International Journal of Biology and Life Sciences 2, no. 3 (2023): 12–15. http://dx.doi.org/10.54097/ijbls.v2i3.8644.

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Both cellular senescence and cytoskeleton are involved in the formation of many diseases and cell signaling pathways. Although recent studies have shown that F-actin is involved in DNA damage repair, chromatin decompression, gene transcription regulation, and cell fate determination. But studies on F-actin and aging are still absence. It is unclear whether nuclear F-actin is present during cellular senescence. Here, by confocal optical sectioning and time-lapse imaging, we found acitn chrommobody-TagGFP2-NLS shows the beneficial on investigating senescent human fibroblast IMR-90 cells. To indu

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13

JAMES, Marianne F., Nitasha MANCHANDA, Charo GONZALEZ-AGOSTI, John H. HARTWIG, and Vijaya RAMESH. "The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association." Biochemical Journal 356, no. 2 (2001): 377–86. http://dx.doi.org/10.1042/bj3560377.

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The neurofibromatosis 2 protein product merlin, named for its relatedness to the ezrin, radixin and moesin (ERM) family of proteins, is a tumour suppressor whose absence results in the occurrence of multiple tumours of the nervous system, particularly schwannomas and meningiomas. Merlin's similarity to ERMs suggests that it might share functions, acting as a link between cytoskeletal components and the cell membrane. The N-terminus of merlin has strong sequence identity to the N-terminal actin-binding region of ezrin; here we describe in detail the merlin–actin interaction. Employing standard

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14

Wei, Mian, Xiaoying Fan, Miao Ding, et al. "Nuclear actin regulates inducible transcription by enhancing RNA polymerase II clustering." Science Advances 6, no. 16 (2020): eaay6515. http://dx.doi.org/10.1126/sciadv.aay6515.

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Gene expression in response to stimuli underlies many fundamental processes. However, how transcription is regulated under these scenarios is largely unknown. Here, we find a previously unknown role of nuclear actin in transcriptional regulation. The RNA-seq data reveal that nuclear actin is required for the serum-induced transcriptional program. Using super-resolution imaging, we found a remarkable enhancement of RNA polymerase II (Pol II) clustering upon serum stimulation, and this enhancement requires nuclear actin. Pol II clusters colocalized with the serum-response genes and nuclear actin

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15

Chen, Yuejun, Feifei Wang, Hui Long, Ying Chen, Ziyan Wu, and Lan Ma. "GRK5 promotes F-actin bundling and targets bundles to membrane structures to control neuronal morphogenesis." Journal of Cell Biology 194, no. 6 (2011): 905–20. http://dx.doi.org/10.1083/jcb.201104114.

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Neuronal morphogenesis requires extensive membrane remodeling and cytoskeleton dynamics. In this paper, we show that GRK5, a G protein–coupled receptor kinase, is critically involved in neurite outgrowth, dendrite branching, and spine morphogenesis through promotion of filopodial protrusion. Interestingly, GRK5 is not acting as a kinase but rather provides a key link between the plasma membrane and the actin cytoskeleton. GRK5 promoted filamentous actin (F-actin) bundling at the membranes of dynamic neuronal structures by interacting with both F-actin and phosphatidylinositol-4,5-bisphosphate.

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16

Vaduva, Gabriela, Nancy C. Martin, and Anita K. Hopper. "Actin-binding Verprolin Is a Polarity Development Protein Required for the Morphogenesis and Function of the Yeast Actin Cytoskeleton." Journal of Cell Biology 139, no. 7 (1997): 1821–33. http://dx.doi.org/10.1083/jcb.139.7.1821.

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Yeast verprolin, encoded by VRP1, is implicated in cell growth, cytoskeletal organization, endocytosis and mitochondrial protein distribution and function. We show that verprolin is also required for bipolar bud-site selection. Previously we reported that additional actin suppresses the temperature-dependent growth defect caused by a mutation in VRP1. Here we show that additional actin suppresses all known defects caused by vrp1-1 and conclude that the defects relate to an abnormal cytoskeleton. Using the two-hybrid system, we show that verprolin binds actin. An actin-binding domain maps to th

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17

Egea, Gustavo, Carla Serra-Peinado, Laia Salcedo-Sicilia, and Enric Gutiérrez-Martínez. "Actin acting at the Golgi." Histochemistry and Cell Biology 140, no. 3 (2013): 347–60. http://dx.doi.org/10.1007/s00418-013-1115-8.

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18

Le Moigne, Ronan, Frédéric Subra, Manale Karam та Christian Auclair. "The β-carboline Harmine Induces Actin Dynamic Remodeling and Abrogates the Malignant Phenotype in Tumorigenic Cells". Cells 9, № 5 (2020): 1168. http://dx.doi.org/10.3390/cells9051168.

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Numerous studies have shown that alteration of actin remodeling plays a pivotal role in the regulation of morphologic and phenotypic changes leading to malignancy. In the present study, we searched for drugs that can regulate actin polymerization and reverse the malignant phenotype in cancer cells. We developed a cell-free high-throughput screening assay for the identification of compounds that induce the actin polymerization in vitro, by fluorescence anisotropy. Then, the potential of the hit compound to restore the actin cytoskeleton and reverse the malignant phenotype was checked in EWS-Fli

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19

Grandy, Carolin, Fabian Port, Jonas Pfeil, and Kay-Eberhard Gottschalk. "Influence of ROCK Pathway Manipulation on the Actin Cytoskeleton Height." Cells 11, no. 3 (2022): 430. http://dx.doi.org/10.3390/cells11030430.

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The actin cytoskeleton with its dynamic properties serves as the driving force for the movement and division of cells and gives the cell shape and structure. Disorders in the actin cytoskeleton occur in many diseases. Deeper understanding of its regulation is essential in order to better understand these biochemical processes. In our study, we use metal-induced energy transfer (MIET) as a tool to quantitatively examine the rarely considered third dimension of the actin cytoskeleton with nanometer accuracy. In particular, we investigate the influence of different drugs acting on the ROCK pathwa

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20

Chitu, Violeta, Fiona J. Pixley, Frank Macaluso, et al. "The PCH Family Member MAYP/PSTPIP2 Directly Regulates F-Actin Bundling and Enhances Filopodia Formation and Motility in Macrophages." Molecular Biology of the Cell 16, no. 6 (2005): 2947–59. http://dx.doi.org/10.1091/mbc.e04-10-0914.

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Macrophage actin-associated tyrosine phosphorylated protein (MAYP) belongs to the Pombe Cdc15 homology (PCH) family of proteins involved in the regulation of actin-based functions including cell adhesion and motility. In mouse macrophages, MAYP is tyrosine phosphorylated after activation of the colony-stimulating factor-1 receptor (CSF-1R), which also induces actin reorganization, membrane ruffling, cell spreading, polarization, and migration. Because MAYP associates with F-actin, we investigated the function of MAYP in regulating actin organization in macrophages. Overexpression of MAYP decre

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21

Saarikangas, Juha, Hongxia Zhao, and Pekka Lappalainen. "Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides." Physiological Reviews 90, no. 1 (2010): 259–89. http://dx.doi.org/10.1152/physrev.00036.2009.

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The plasma membrane and the underlying cortical actin cytoskeleton undergo continuous dynamic interplay that is responsible for many essential aspects of cell physiology. Polymerization of actin filaments against cellular membranes provides the force for a number of cellular processes such as migration, morphogenesis, and endocytosis. Plasma membrane phosphoinositides (especially phosphatidylinositol bis- and trisphosphates) play a central role in regulating the organization and dynamics of the actin cytoskeleton by acting as platforms for protein recruitment, by triggering signaling cascades,

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22

Mullins, R. Dyche, Joseph F. Kelleher, and Thomas D. Pollard. "Actin' like actin?" Trends in Cell Biology 6, no. 6 (1996): 208–12. http://dx.doi.org/10.1016/0962-8924(96)20017-0.

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23

Verma, Suzie, Siew Ping Han, Magdalene Michael, et al. "A WAVE2–Arp2/3 actin nucleator apparatus supports junctional tension at the epithelial zonula adherens." Molecular Biology of the Cell 23, no. 23 (2012): 4601–10. http://dx.doi.org/10.1091/mbc.e12-08-0574.

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The epithelial zonula adherens (ZA) is a specialized adhesive junction where actin dynamics and myosin-driven contractility coincide. The junctional cytoskeleton is enriched in myosin II, which generates contractile force to support junctional tension. It is also enriched in dynamic actin filaments, which are replenished by ongoing actin assembly. In this study we sought to pursue the relationship between actin assembly and junctional contractility. We demonstrate that WAVE2–Arp2/3 is a major nucleator of actin assembly at the ZA and likely acts in response to junctional Rac signaling. Further

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24

Chiu, Tim Ting, Nish Patel, Alisa E. Shaw, James R. Bamburg, and Amira Klip. "Arp2/3- and Cofilin-coordinated Actin Dynamics Is Required for Insulin-mediated GLUT4 Translocation to the Surface of Muscle Cells." Molecular Biology of the Cell 21, no. 20 (2010): 3529–39. http://dx.doi.org/10.1091/mbc.e10-04-0316.

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GLUT4 vesicles are actively recruited to the muscle cell surface upon insulin stimulation. Key to this process is Rac-dependent reorganization of filamentous actin beneath the plasma membrane, but the underlying molecular mechanisms have yet to be elucidated. Using L6 rat skeletal myoblasts stably expressing myc-tagged GLUT4, we found that Arp2/3, acting downstream of Rac GTPase, is responsible for the cortical actin polymerization evoked by insulin. siRNA-mediated silencing of either Arp3 or p34 subunits of the Arp2/3 complex abrogated actin remodeling and impaired GLUT4 translocation. Insuli

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25

Schüler, Herwig, and Kai Matuschewski. "Plasmodium motility: actin not actin' like actin." Trends in Parasitology 22, no. 4 (2006): 146–47. http://dx.doi.org/10.1016/j.pt.2006.02.005.

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26

Ly, Thu, Natalia Moroz, Christopher T. Pappas, et al. "The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2’s function." Molecular Biology of the Cell 27, no. 16 (2016): 2565–75. http://dx.doi.org/10.1091/mbc.e16-03-0200.

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Leiomodin is a potent actin nucleator related to tropomodulin, a capping protein localized at the pointed end of the thin filaments. Mutations in leiomodin-3 are associated with lethal nemaline myopathy in humans, and leiomodin-2–knockout mice present with dilated cardiomyopathy. The arrangement of the N-terminal actin- and tropomyosin-binding sites in leiomodin is contradictory and functionally not well understood. Using one-dimensional nuclear magnetic resonance and the pointed-end actin polymerization assay, we find that leiomodin-2, a major cardiac isoform, has an N-terminal actin-binding

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27

Cingolani, Lorenzo A., and Yukiko Goda. "Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy." Nature Reviews Neuroscience 9, no. 5 (2008): 344–56. http://dx.doi.org/10.1038/nrn2373.

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28

Jégou, Antoine, and Guillaume Romet-Lemonne. "Mechanically tuning actin filaments to modulate the action of actin-binding proteins." Current Opinion in Cell Biology 68 (February 2021): 72–80. http://dx.doi.org/10.1016/j.ceb.2020.09.002.

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29

Lechler, Terry, and Rong Li. "In Vitro Reconstitution of Cortical Actin Assembly Sites in Budding Yeast." Journal of Cell Biology 138, no. 1 (1997): 95–103. http://dx.doi.org/10.1083/jcb.138.1.95.

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We have developed a biochemical approach for identifying the components of cortical actin assembly sites in polarized yeast cells, based on a permeabilized cell assay that we established for actin assembly in vitro. Previous analysis indicated that an activity associated with the cell cortex promotes actin polymerization in the bud. After inactivation by a chemical treatment, this activity can be reconstituted back to the permeabilized cells from a cytoplasmic extract. Fractionation of the extract revealed that the reconstitution depends on two sequentially acting protein factors. Bee1, a cort

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30

Nishimura, Kazunari, Fumie Yoshihara, Takuro Tojima, et al. "L1-dependent neuritogenesis involves ankyrinB that mediates L1-CAM coupling with retrograde actin flow." Journal of Cell Biology 163, no. 5 (2003): 1077–88. http://dx.doi.org/10.1083/jcb.200303060.

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The cell adhesion molecule L1 (L1-CAM) plays critical roles in neurite growth. Its cytoplasmic domain (L1CD) binds to ankyrins that associate with the spectrin–actin network. This paper demonstrates that L1-CAM interactions with ankyrinB (but not with ankyrinG) are involved in the initial formation of neurites. In the membranous protrusions surrounding the soma before neuritogenesis, filamentous actin (F-actin) and ankyrinB continuously move toward the soma (retrograde flow). Bead-tracking experiments show that ankyrinB mediates L1-CAM coupling with retrograde F-actin flow in these perisomatic

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31

Alonso-Sanz, Ramón, and Andy Adamatzky. "Actin Automata with Memory." International Journal of Bifurcation and Chaos 26, no. 01 (2016): 1650019. http://dx.doi.org/10.1142/s021812741650019x.

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Actin is a globular protein which forms long polar filaments in eukaryotic. The actin filaments play the roles of cytoskeleton, motility units, information processing and learning. We model actin filament as a double chain of finite state machines, nodes, which take states “0” and “1”. The states are abstractions of absence and presence of a subthreshold charge on actin units corresponding to the nodes. All nodes update their state in parallel to discrete time. A node updates its current state depending on states of two closest neighbors in the node chain and two closest neighbors in the compl

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32

Fabrice, Tohnyui Ndinyanka, Thomas Fiedler, Vera Studer, et al. "Interactome and F-Actin Interaction Analysis of Dictyostelium discoideum Coronin A." International Journal of Molecular Sciences 21, no. 4 (2020): 1469. http://dx.doi.org/10.3390/ijms21041469.

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Coronin proteins are evolutionary conserved WD repeat containing proteins that have been proposed to carry out different functions. In Dictyostelium, the short coronin isoform, coronin A, has been implicated in cytoskeletal reorganization, chemotaxis, phagocytosis and the initiation of multicellular development. Generally thought of as modulators of F-actin, coronin A and its mammalian homologs have also been shown to mediate cellular processes in an F-actin-independent manner. Therefore, it remains unclear whether or not coronin A carries out its functions through its capacity to interact wit

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33

Zeidman, Ruth, Ulrika Trollér, Arathi Raghunath, Sven Påhlman та Christer Larsson. "Protein Kinase Cε Actin-binding Site Is Important for Neurite Outgrowth during Neuronal Differentiation". Molecular Biology of the Cell 13, № 1 (2002): 12–24. http://dx.doi.org/10.1091/mbc.01-04-0210.

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We have previously shown that protein kinase Cε (PKCε) induces neurite outgrowth via its regulatory domain and independently of its kinase activity. This study aimed at identifying mechanisms regulating PKCε-mediated neurite induction. We show an increased association of PKCε to the cytoskeleton during neuronal differentiation. Furthermore, neurite induction by overexpression of full-length PKCε is suppressed if serum is removed from the cultures or if an actin-binding site is deleted from the protein. A peptide corresponding to the PKCε actin-binding site suppresses neurite outgrowth during n

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34

Egile, Coumaran, Thomas P. Loisel, Valérie Laurent, et al. "Activation of the Cdc42 Effector N-Wasp by the Shigella flexneri Icsa Protein Promotes Actin Nucleation by Arp2/3 Complex and Bacterial Actin-Based Motility." Journal of Cell Biology 146, no. 6 (1999): 1319–32. http://dx.doi.org/10.1083/jcb.146.6.1319.

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To propel itself in infected cells, the pathogen Shigella flexneri subverts the Cdc42-controlled machinery responsible for actin assembly during filopodia formation. Using a combination of bacterial motility assays in platelet extracts with Escherichia coli expressing the Shigella IcsA protein and in vitro analysis of reconstituted systems from purified proteins, we show here that the bacterial protein IcsA binds N-WASP and activates it in a Cdc42-like fashion. Dramatic stimulation of actin assembly is linked to the formation of a ternary IcsA–N-WASP–Arp2/3 complex, which nucleates actin polym

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35

Adler, E. M. "Acting with Actin (But Not Akt)." Science Signaling 4, no. 178 (2011): ec169-ec169. http://dx.doi.org/10.1126/scisignal.4178ec169.

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36

Cingolani, Lorenzo A., and Yukiko Goda. "Erratum: Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy." Nature Reviews Neuroscience 9, no. 6 (2008): 494. http://dx.doi.org/10.1038/nrn2410.

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37

Quitschke, W. W., L. DePonti-Zilli, Z. Y. Lin, and B. M. Paterson. "Identification of two nuclear factor-binding domains on the chicken cardiac actin promoter: implications for regulation of the gene." Molecular and Cellular Biology 9, no. 8 (1989): 3218–30. http://dx.doi.org/10.1128/mcb.9.8.3218-3230.1989.

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The cis-acting regions that appear to be involved in negative regulation of the chicken alpha-cardiac actin promoter both in vivo and in vitro have been identified. A nuclear factor(s) binding to the proximal region mapped over the TATA element between nucleotides -50 and -25. In the distal region, binding spanned nucleotides -136 to -112, a region that included a second CArG box (CArG2) 5' to the more familiar CCAAT-box (CArG1) consensus sequence. Nuclear factors binding to these different domains were found in both muscle and nonmuscle preparations but were detectable at considerably lower l

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38

Quitschke, W. W., L. DePonti-Zilli, Z. Y. Lin, and B. M. Paterson. "Identification of two nuclear factor-binding domains on the chicken cardiac actin promoter: implications for regulation of the gene." Molecular and Cellular Biology 9, no. 8 (1989): 3218–30. http://dx.doi.org/10.1128/mcb.9.8.3218.

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The cis-acting regions that appear to be involved in negative regulation of the chicken alpha-cardiac actin promoter both in vivo and in vitro have been identified. A nuclear factor(s) binding to the proximal region mapped over the TATA element between nucleotides -50 and -25. In the distal region, binding spanned nucleotides -136 to -112, a region that included a second CArG box (CArG2) 5' to the more familiar CCAAT-box (CArG1) consensus sequence. Nuclear factors binding to these different domains were found in both muscle and nonmuscle preparations but were detectable at considerably lower l

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39

French, B. A., K. L. Chow, E. N. Olson, and R. J. Schwartz. "Heterodimers of myogenic helix-loop-helix regulatory factors and E12 bind a complex element governing myogenic induction of the avian cardiac alpha-actin promoter." Molecular and Cellular Biology 11, no. 5 (1991): 2439–50. http://dx.doi.org/10.1128/mcb.11.5.2439-2450.1991.

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Recent studies have shown that two genes regulating myogenesis (MyoD and myogenin) are coexpressed with cardiac alpha-actin during early stages of skeletal muscle development. Myogenin and MyoD are members of a family of regulatory proteins which share a helix-loop-helix (HLH) motif required for dimerization and DNA binding. Myogenin and MyoD form heterodimers with the ubiquitous HLH protein E12 which bind cis-acting DNA elements that have an E box (CANNTG) at their core. E boxes are present in the control regions of numerous muscle-specific genes, although their functional importance in regul

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40

French, B. A., K. L. Chow, E. N. Olson, and R. J. Schwartz. "Heterodimers of myogenic helix-loop-helix regulatory factors and E12 bind a complex element governing myogenic induction of the avian cardiac alpha-actin promoter." Molecular and Cellular Biology 11, no. 5 (1991): 2439–50. http://dx.doi.org/10.1128/mcb.11.5.2439.

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Recent studies have shown that two genes regulating myogenesis (MyoD and myogenin) are coexpressed with cardiac alpha-actin during early stages of skeletal muscle development. Myogenin and MyoD are members of a family of regulatory proteins which share a helix-loop-helix (HLH) motif required for dimerization and DNA binding. Myogenin and MyoD form heterodimers with the ubiquitous HLH protein E12 which bind cis-acting DNA elements that have an E box (CANNTG) at their core. E boxes are present in the control regions of numerous muscle-specific genes, although their functional importance in regul

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41

Pollard, Thomas D. "Actin and Actin-Binding Proteins." Cold Spring Harbor Perspectives in Biology 8, no. 8 (2016): a018226. http://dx.doi.org/10.1101/cshperspect.a018226.

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42

Sameshima, Masazumi, Yoshiro Kishi, Masako Osumi, Dana Mahadeo, and David A. Cotter. "Novel Actin Cytoskeleton. Actin Tubules." Cell Structure and Function 25, no. 5 (2000): 291–95. http://dx.doi.org/10.1247/csf.25.291.

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43

Fagraeus, Astrid. "Actin and anti-actin antibodies." Clinical Immunology Newsletter 6, no. 6 (1985): 93–94. http://dx.doi.org/10.1016/s0197-1859(85)80028-5.

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44

Bugalhão, Joana N., Luís Jaime Mota, and Irina S. Franco. "Bacterial nucleators: actin' on actin." Pathogens and Disease 73, no. 9 (2015): ftv078. http://dx.doi.org/10.1093/femspd/ftv078.

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Ampe, Christophe, and Joël Vandekerckhove. "Actin-actin binding protein interfaces." Seminars in Cell Biology 5, no. 3 (1994): 175–82. http://dx.doi.org/10.1006/scel.1994.1022.

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Papakonstanti, Evangelia A., and Christos Stournaras. "Association of PI-3 Kinase with PAK1 Leads to Actin Phosphorylation and Cytoskeletal Reorganization." Molecular Biology of the Cell 13, no. 8 (2002): 2946–62. http://dx.doi.org/10.1091/mbc.02-01-0599.

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The family of p21-activated kinases (PAKs) have been implicated in the rearrangement of actin cytoskeleton by acting downstream of the small GTPases Rac and Cdc42. Here we report that even though Cdc42/Rac1 or Akt are not activated, phosphatidylinositol-3 (PI-3) kinase activation induces PAK1 kinase activity. Indeed, we demonstrate that PI-3 kinase associates with the N-terminal regulatory domain of PAK1 (amino acids 67–150) leading to PAK1 activation. The association of the PI-3 kinase with the Cdc42/Rac1 binding-deficient PAK1(H83,86L) confirms that the small GTPases are not involved in the

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Chen, Hsin, Chun-Chen Kuo, Hui Kang, et al. "Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p." Molecular Biology of the Cell 23, no. 19 (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

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Wolgemuth, Charles W., and Sean X. Sun. "Active random forces can drive differential cellular positioning and enhance motor-driven transport." Molecular Biology of the Cell 31, no. 20 (2020): 2283–88. http://dx.doi.org/10.1091/mbc.e19-11-0629.

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Bergsma, D. J., J. M. Grichnik, L. M. Gossett, and R. J. Schwartz. "Delimitation and characterization of cis-acting DNA sequences required for the regulated expression and transcriptional control of the chicken skeletal alpha-actin gene." Molecular and Cellular Biology 6, no. 7 (1986): 2462–75. http://dx.doi.org/10.1128/mcb.6.7.2462-2475.1986.

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We have previously observed that DNA sequences within the 5'-flanking region of the chicken skeletal alpha-actin gene harbor a cis-acting regulatory element that influences cell type and developmental stage-specific expression (J. M. Grichnik, D. J. Bergsma, and R. J. Schwartz, Nucleic Acids Res 14:1683-1701, 1986). In this report we have constructed unidirectional 5'-deletion and region-specific deletion-insertion mutations of the chicken skeletal alpha-actin upstream region and inserted these into the chloramphenicol acetyltransferase expression vector pSV0CAT. These constructions were used

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Bergsma, D. J., J. M. Grichnik, L. M. Gossett, and R. J. Schwartz. "Delimitation and characterization of cis-acting DNA sequences required for the regulated expression and transcriptional control of the chicken skeletal alpha-actin gene." Molecular and Cellular Biology 6, no. 7 (1986): 2462–75. http://dx.doi.org/10.1128/mcb.6.7.2462.

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Abstract:

We have previously observed that DNA sequences within the 5'-flanking region of the chicken skeletal alpha-actin gene harbor a cis-acting regulatory element that influences cell type and developmental stage-specific expression (J. M. Grichnik, D. J. Bergsma, and R. J. Schwartz, Nucleic Acids Res 14:1683-1701, 1986). In this report we have constructed unidirectional 5'-deletion and region-specific deletion-insertion mutations of the chicken skeletal alpha-actin upstream region and inserted these into the chloramphenicol acetyltransferase expression vector pSV0CAT. These constructions were used

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