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Artículos de revistas sobre el tema "Actin cytoskeleton"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 26 de julio de 2025

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1

Liu, Yi, Keyvan Mollaeian, and Juan Ren. "An Image Recognition-Based Approach to Actin Cytoskeleton Quantification." Electronics 7, no. 12 (2018): 443. http://dx.doi.org/10.3390/electronics7120443.

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Quantification of the actin cytoskeleton is of prime importance to unveil the cellular force sensing and transduction mechanism. Although fluorescence imaging provides a convenient tool for observing the morphology of the actin cytoskeleton, due to the lack of approaches to accurate actin cytoskeleton quantification, the dynamics of mechanotransduction is still poorly understood. Currently, the existing image-based actin cytoskeleton analysis tools are either incapable of quantifying both the orientation and the quantity of the actin cytoskeleton simultaneously or the quantified results are su

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2

Breuer, David, Alexander Ivakov, Arun Sampathkumar, Florian Hollandt, Staffan Persson, and Zoran Nikoloski. "Quantitative analyses of the plant cytoskeleton reveal underlying organizational principles." Journal of The Royal Society Interface 11, no. 97 (2014): 20140362. http://dx.doi.org/10.1098/rsif.2014.0362.

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The actin and microtubule (MT) cytoskeletons are vital structures for cell growth and development across all species. While individual molecular mechanisms underpinning actin and MT dynamics have been intensively studied, principles that govern the cytoskeleton organization remain largely unexplored. Here, we captured biologically relevant characteristics of the plant cytoskeleton through a network-driven imaging-based approach allowing us to quantitatively assess dynamic features of the cytoskeleton. By introducing suitable null models, we demonstrate that the plant cytoskeletal networks exhi

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3

Jack, R. M., R. M. Ezzell, J. Hartwig, and D. T. Fearon. "Differential interaction of the C3b/C4b receptor and MHC class I with the cytoskeleton of human neutrophils." Journal of Immunology 137, no. 12 (1986): 3996–4003. http://dx.doi.org/10.4049/jimmunol.137.12.3996.

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Abstract As measured by fluorescence microscopy and radioligand binding, C3b/C4b receptors (CR1) became attached to the detergent-insoluble cytoskeleton of human neutrophils when receptors were cross-linked by affinity-purified polyclonal F(ab')2 anti-CR1, dimeric C3b, or Fab monoclonal anti-CR1 followed by F(ab')2 goat anti-mouse F(ab')2. CR1 on neutrophils bearing monovalent anti-CR1 was not attached to the cytoskeleton. In contrast, cross-linked CR1 on erythrocytes and cross-linked MHC Class I on neutrophils were not cytoskeleton associated. A possible role for filamentous actin (F-actin) i

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4

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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5

Bezanilla, Magdalena, Amy S. Gladfelter, David R. Kovar, and Wei-Lih Lee. "Cytoskeletal dynamics: A view from the membrane." Journal of Cell Biology 209, no. 3 (2015): 329–37. http://dx.doi.org/10.1083/jcb.201502062.

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Many aspects of cytoskeletal assembly and dynamics can be recapitulated in vitro; yet, how the cytoskeleton integrates signals in vivo across cellular membranes is far less understood. Recent work has demonstrated that the membrane alone, or through membrane-associated proteins, can effect dynamic changes to the cytoskeleton, thereby impacting cell physiology. Having identified mechanistic links between membranes and the actin, microtubule, and septin cytoskeletons, these studies highlight the membrane’s central role in coordinating these cytoskeletal systems to carry out essential processes,

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6

SAUMET, Anne, Nando de JESUS, Chantal LEGRAND та Véronique DUBERNARD. "Association of thrombospondin-1 with the actin cytoskeleton of human thrombin-activated platelets through an αIIbβ3- or CD36-independent mechanism". Biochemical Journal 363, № 3 (2002): 473–82. http://dx.doi.org/10.1042/bj3630473.

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Thrombospondin-1 (TSP-1) is an adhesive glycoprotein which, when secreted from α-granules of activated platelets, can bind to the cell surface and participate in platelet aggregate formation. In this study, we show that thrombin activation leads to the rapid and specific association of a large amount of secreted α-granular TSP-1 with the actin cytoskeleton. This cytoskeletal association of TSP-1 was correlated with platelet secretion, but not aggregation, and was inhibited by cytochalasin D, an inhibitor of actin polymerization. Association of TSP-1 with the actin cytoskeleton was mediated by

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7

Ballestrem, C., B. Wehrle-Haller, and B. A. Imhof. "Actin dynamics in living mammalian cells." Journal of Cell Science 111, no. 12 (1998): 1649–58. http://dx.doi.org/10.1242/jcs.111.12.1649.

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The actin cytoskeleton maintains the cellular architecture and mediates cell movements. To explore actin cytoskeletal dynamics, the enhanced green fluorescent protein (EGFP) was fused to human β-actin. The fusion protein was incorporated into actin fibers which became depolymerized upon cytochalasin B treatment. This functional EGFP-actin construct enabled observation of the actin cytoskeleton in living cells by time lapse fluorescence microscopy. Stable expression of the construct was obtained in mammalian cell lines of different tissue origins. In stationary cells, actin rich, ring-like stru

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8

Holly, Stephen P., and Kendall J. Blumer. "Pak-Family Kinases Regulate Cell and Actin Polarization Throughout the Cell Cycle of Saccharomyces cerevisiae." Journal of Cell Biology 147, no. 4 (1999): 845–56. http://dx.doi.org/10.1083/jcb.147.4.845.

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During the cell cycle of the yeast Saccharomyces cerevisiae, the actin cytoskeleton and cell surface growth are polarized, mediating bud emergence, bud growth, and cytokinesis. We have determined whether p21-activated kinase (PAK)-family kinases regulate cell and actin polarization at one or several points during the yeast cell cycle. Inactivation of the PAK homologues Ste20 and Cla4 at various points in the cell cycle resulted in loss of cell and actin cytoskeletal polarity, but not in depolymerization of F-actin. Loss of PAK function in G1 depolarized the cortical actin cytoskeleton and bloc

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9

Uray, Karen, Evelin Major, and Beata Lontay. "MicroRNA Regulatory Pathways in the Control of the Actin–Myosin Cytoskeleton." Cells 9, no. 7 (2020): 1649. http://dx.doi.org/10.3390/cells9071649.

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MicroRNAs (miRNAs) are key modulators of post-transcriptional gene regulation in a plethora of processes, including actin–myosin cytoskeleton dynamics. Recent evidence points to the widespread effects of miRNAs on actin–myosin cytoskeleton dynamics, either directly on the expression of actin and myosin genes or indirectly on the diverse signaling cascades modulating cytoskeletal arrangement. Furthermore, studies from various human models indicate that miRNAs contribute to the development of various human disorders. The potentially huge impact of miRNA-based mechanisms on cytoskeletal elements

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10

Vindin, Howard, Leanne Bischof, Peter Gunning, and Justine Stehn. "Validation of an Algorithm to Quantify Changes in Actin Cytoskeletal Organization." Journal of Biomolecular Screening 19, no. 3 (2013): 354–68. http://dx.doi.org/10.1177/1087057113503494.

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The actin cytoskeleton plays an important role in most, if not all, processes necessary for cell survival. Given the fundamental role that the actin cytoskeleton plays in the progression of cancer, it is an ideal target for chemotherapy. Although it is possible to image the actin cytoskeleton in a high-throughput manner, there is currently no validated method to quantify changes in the cytoskeleton in the same capacity, which makes research into its organization and the development of anticytoskeletal drugs difficult. We have validated the use of a linear feature detection algorithm, allowing

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11

Jones, Steven L., and Tatyana M. Svitkina. "Axon Initial Segment Cytoskeleton: Architecture, Development, and Role in Neuron Polarity." Neural Plasticity 2016 (2016): 1–19. http://dx.doi.org/10.1155/2016/6808293.

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The axon initial segment (AIS) is a specialized structure in neurons that resides in between axonal and somatodendritic domains. The localization of the AIS in neurons is ideal for its two major functions: it serves as the site of action potential firing and helps to maintain neuron polarity. It has become increasingly clear that the AIS cytoskeleton is fundamental to AIS functions. In this review, we discuss current understanding of the AIS cytoskeleton with particular interest in its unique architecture and role in maintenance of neuron polarity. The AIS cytoskeleton is divided into two part

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12

Breuer, David, Jacqueline Nowak, Alexander Ivakov, Marc Somssich, Staffan Persson, and Zoran Nikoloski. "System-wide organization of actin cytoskeleton determines organelle transport in hypocotyl plant cells." Proceedings of the National Academy of Sciences 114, no. 28 (2017): E5741—E5749. http://dx.doi.org/10.1073/pnas.1706711114.

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The actin cytoskeleton is an essential intracellular filamentous structure that underpins cellular transport and cytoplasmic streaming in plant cells. However, the system-level properties of actin-based cellular trafficking remain tenuous, largely due to the inability to quantify key features of the actin cytoskeleton. Here, we developed an automated image-based, network-driven framework to accurately segment and quantify actin cytoskeletal structures and Golgi transport. We show that the actin cytoskeleton in both growing and elongated hypocotyl cells has structural properties facilitating ef

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13

Liu, Lingling, Qing Luo, Jinghui Sun, and Guanbin Song. "Cytoskeletal control of nuclear morphology and stiffness are required for OPN-induced bone-marrow-derived mesenchymal stem cell migration." Biochemistry and Cell Biology 97, no. 4 (2019): 463–70. http://dx.doi.org/10.1139/bcb-2018-0263.

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During cell migration, the movement of the nucleus must be coordinated with the cytoskeletal dynamics that influence the efficiency of cell migration. Our previous study demonstrated that osteopontin (OPN) significantly promotes the migration of bone-marrow-derived mesenchymal stem cells (BMSCs). However, the mechanism that regulates nuclear mechanics of the cytoskeleton during OPN-promoted BMSC migration remains unclear. In this study, we investigated how the actin cytoskeleton influences nuclear mechanics in BMSCs. We assessed the morphology and mechanics of the nuclei in the OPN-treated BMS

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14

Akram, Zain, Ishtiaq Ahmed, Heike Mack, et al. "Yeast as a Model to Understand Actin-Mediated Cellular Functions in Mammals—Illustrated with Four Actin Cytoskeleton Proteins." Cells 9, no. 3 (2020): 672. http://dx.doi.org/10.3390/cells9030672.

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The budding yeast Saccharomyces cerevisiae has an actin cytoskeleton that comprises a set of protein components analogous to those found in the actin cytoskeletons of higher eukaryotes. Furthermore, the actin cytoskeletons of S. cerevisiae and of higher eukaryotes have some similar physiological roles. The genetic tractability of budding yeast and the availability of a stable haploid cell type facilitates the application of molecular genetic approaches to assign functions to the various actin cytoskeleton components. This has provided information that is in general complementary to that provid

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15

Aunis, D., and M. F. Bader. "The cytoskeleton as a barrier to exocytosis in secretory cells." Journal of Experimental Biology 139, no. 1 (1988): 253–66. http://dx.doi.org/10.1242/jeb.139.1.253.

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Chromaffin cells of the adrenal medulla synthesize, store and secrete catecholamines. These cells contain numerous electron-dense secretory granules which discharge their contents into the extracellular space by exocytosis. The subplasmalemmal area of the chromaffin cell is characterized by the presence of a highly organized cytoskeletal network. F-Actin seems to be exclusively localized in this area and together with specific actin-binding proteins forms a dense viscoelastic gel; fodrin, vinculin and caldesmon, three actin cross-linking proteins, and gelsolin, an actin-severing protein, are f

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16

Liu, Yi-Jun, Ting Zhang, Daxiao Cheng, et al. "Late endosomes promote microglia migration via cytosolic translocation of immature protease cathD." Science Advances 6, no. 50 (2020): eaba5783. http://dx.doi.org/10.1126/sciadv.aba5783.

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Organelle transport requires dynamic cytoskeleton remodeling, but whether cytoskeletal dynamics are, in turn, regulated by organelles remains elusive. Here, we demonstrate that late endosomes, a type of prelysosomal organelles, facilitate actin-cytoskeleton remodeling via cytosolic translocation of immature protease cathepsin D (cathD) during microglia migration. After cytosolic translocation, late endosome–derived cathD juxtaposes actin filaments at the leading edge of lamellipodia. Suppressing cathD expression or blocking its cytosolic translocation impairs the maintenance but not the initia

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17

Harris, Andrew R., Pamela Jreij, and Daniel A. Fletcher. "Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals." Annual Review of Biophysics 47, no. 1 (2018): 617–31. http://dx.doi.org/10.1146/annurev-biophys-070816-033547.

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Force transmission through the actin cytoskeleton plays a central role in cell movements, shape change, and internal organization. Dynamic reorganization of actin filaments by an array of specialized binding proteins creates biochemically and architecturally distinct structures, many of which are finely tuned to exert or resist mechanical loads. The molecular complexity of the actin cytoskeleton continues to be revealed by detailed biochemical assays, and the architectural diversity and dynamics of actin structures are being uncovered by advances in super-resolution fluorescence microscopy and

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18

Durand-Smet, Pauline, Tamsin A. Spelman, Elliot M. Meyerowitz, and Henrik Jönsson. "Cytoskeletal organization in isolated plant cells under geometry control." Proceedings of the National Academy of Sciences 117, no. 29 (2020): 17399–408. http://dx.doi.org/10.1073/pnas.2003184117.

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The cytoskeleton plays a key role in establishing robust cell shape. In animals, it is well established that cell shape can also influence cytoskeletal organization. Cytoskeletal proteins are well conserved between animal and plant kingdoms; nevertheless, because plant cells exhibit major structural differences to animal cells, the question arises whether the plant cytoskeleton also responds to geometrical cues. Recent numerical simulations predicted that a geometry-based rule is sufficient to explain the microtubule (MT) organization observed in cells. Due to their high flexural rigidity and

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19

Swaminathan, Vinay, Joseph Mathew Kalappurakkal, Shalin B. Mehta, et al. "Actin retrograde flow actively aligns and orients ligand-engaged integrins in focal adhesions." Proceedings of the National Academy of Sciences 114, no. 40 (2017): 10648–53. http://dx.doi.org/10.1073/pnas.1701136114.

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Integrins are transmembrane receptors that, upon activation, bind extracellular ligands and link them to the actin filament (F-actin) cytoskeleton to mediate cell adhesion and migration. Cytoskeletal forces in migrating cells generated by polymerization- or contractility-driven “retrograde flow” of F-actin from the cell leading edge have been hypothesized to mediate integrin activation for ligand binding. This predicts that these forces should align and orient activated, ligand-bound integrins at the leading edge. Here, polarization-sensitive fluorescence microscopy of GFP-αVβ3 integrins in fi

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20

Benoit, Béatrice, Anita Baillet, and Christian Poüs. "Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators." International Journal of Molecular Sciences 22, no. 16 (2021): 8375. http://dx.doi.org/10.3390/ijms22168375.

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This review extensively reports data from the literature concerning the complex relationships between the stress-induced c-Jun N-terminal kinases (JNKs) and the four main cytoskeleton elements, which are actin filaments, microtubules, intermediate filaments, and septins. To a lesser extent, we also focused on the two membrane-associated cytoskeletons spectrin and ESCRT-III. We gather the mechanisms controlling cytoskeleton-associated JNK activation and the known cytoskeleton-related substrates directly phosphorylated by JNK. We also point out specific locations of the JNK upstream regulators a

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21

Li, S., V. C. Duance, and E. J. Blain. "F-actin cytoskeletal organization in intervertebral disc health and disease." Biochemical Society Transactions 35, no. 4 (2007): 683–85. http://dx.doi.org/10.1042/bst0350683.

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The cytoskeleton, which in most cell types, including the intervertebral disc described here, comprises microfilaments, microtubules and intermediate filaments, plays important functions in many fundamental cellular events, including cell division, motility, protein trafficking and secretion. The cytoskeleton is also critical for communication; for example, alterations to the architecture of the F-actin (filamentous actin) cytoskeletal networks can affect communication between the cells and the extracellular matrix, potentially compromising tissue homoeostasis. Although there are limited studi

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22

Nurko, S., K. Sogabe, J. A. Davis, et al. "Contribution of actin cytoskeletal alterations to ATP depletion and calcium-induced proximal tubule cell injury." American Journal of Physiology-Renal Physiology 270, no. 1 (1996): F39—F52. http://dx.doi.org/10.1152/ajprenal.1996.270.1.f39.

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The actin cytoskeleton of rabbit proximal tubules was assessed by deoxyribonuclease (DNase) binding, sedimentability of detergent-insoluble actin, laser-scanning confocal microscopy, and ultrastructure during exposure to hypoxia, antimycin, or antimycin plus ionomycin. One-third of total actin was DNase reactive in control cells prior to deliberate depolymerization, and a similar proportion was unsedimentable from detergent lysates during 2.5 h at 100,000 g. Tubules injured by hypoxia or antimycin alone, without glycine, showed Ca(2+)-dependent pathology of the cytoskeleton, consisting of incr

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23

Templeton, Douglas M., and Ying Liu. "Effects of cadmium on the actin cytoskeleton in renal mesangial cells." Canadian Journal of Physiology and Pharmacology 91, no. 1 (2013): 1–7. http://dx.doi.org/10.1139/cjpp-2012-0229.

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We provide an overview of our studies on cadmium and the actin cytoskeleton in mesangial cells, from earlier work on the effects of Cd2+ on actin polymerization in vivo and in vitro, to a role of disruption or stabilization of the cytoskeleton in apoptosis and apoptosis-like death. More recent studies implicate cadmium-dependent association of gelsolin and the Ca2+/calmodulin-dependent protein kinase II (CaMK-II) with actin filaments in cytoskeletal effects. We also present previously unpublished data concerning cadmium and the disruption of focal adhesions. The work encompasses studies on rat

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24

Kalfa, Theodosia A., Suvarnamala Pushkaran, Narla Mohandas, et al. "Rac GTPases regulate the morphology and deformability of the erythrocyte cytoskeleton." Blood 108, no. 12 (2006): 3637–45. http://dx.doi.org/10.1182/blood-2006-03-005942.

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Abstract Actin oligomers are a significant structural component of the erythrocyte cytoskeleton. Rac1 and Rac2 GTPases regulate actin structures and have multiple overlapping as well as distinct roles in hematopoietic cells; therefore, we studied their role in red blood cells (RBCs). Conditional gene targeting with a loxP-flanked Rac1 gene allowed Crerecombinase–induced deletion of Rac1 on a Rac2 null genetic background. The Rac1–/–;Rac2–/– mice developed microcytic anemia with a hemoglobin drop of about 20% and significant anisocytosis and poikilocytosis. Reticulocytes increased more than 2-f

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25

Payrastre, B., P. M. van Bergen en Henegouwen, M. Breton, et al. "Phosphoinositide kinase, diacylglycerol kinase, and phospholipase C activities associated to the cytoskeleton: effect of epidermal growth factor." Journal of Cell Biology 115, no. 1 (1991): 121–28. http://dx.doi.org/10.1083/jcb.115.1.121.

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In this paper we demonstrate that cytoskeletons isolated from A431 cells have associated with them high activities of several kinases involved in inositol lipid metabolism, such as phosphatidylinositol kinase, phosphatidylinositol phosphate kinase, and diacylglycerol kinase. In addition also phospholipase C activity was detected on isolated cytoskeletons. Controlled extraction of the cytoskeletons followed by in vitro polymerization of actin demonstrated an association of the kinases to the actin filament system consisting of actin and a number of actin-binding proteins. The cytoskeleton-assoc

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26

Wang, Jia, Spencer Freeman, Jeff Lee, and Michael Gold. "Antigen-induced reorientation of the microtubule organizing centre to the B cell immune synapse requires Rap activation and actin dynamics (IRM8P.704)." Journal of Immunology 192, no. 1_Supplement (2014): 127.5. http://dx.doi.org/10.4049/jimmunol.192.supp.127.5.

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Abstract B cell activation can be initiated by antigen presenting cells (APC) that display intact antigen (Ag) on their surface. Reorientation of the B cell microtubule-organizing centre (MTOC) towards the APC facilitates Ag internalization at the immune synapse (IS), which is critical for B cells to present Ag to T cells and elicit T cell help. We showed previously that BCR-induced activation of the Rap GTPase, a key regulator of cell polarity and actin dynamics, is required for IS formation. We now show that BCR-induced Rap activation is critical for MTOC polarization towards anti-Ig-coated

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27

Sechi, A. S., and J. Wehland. "The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane." Journal of Cell Science 113, no. 21 (2000): 3685–95. http://dx.doi.org/10.1242/jcs.113.21.3685.

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The co-ordination of rearrangements of the actin cytoskeleton depends on its tight connection to the plasma membrane. Phosphatidylinositol 4,5-bisphosphate is thought to transmit signals originating at the plasma membrane to the underlying actin cytoskeleton. This lipid binds to, and influences the activity of, several actin-associated proteins in vitro that regulate the architecture of the actin cytoskeleton. Signalling intermediates in this process include focal adhesion molecules such as vinculin and members of two families of proteins, ERM and WASP. These proteins interact with phosphatidy

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28

REDONDO, Pedro C., Ana I. LAJAS, Ginés M. SALIDO, Antonio GONZALEZ, Juan A. ROSADO, and José A. PARIENTE. "Evidence for secretion-like coupling involving pp60src in the activation and maintenance of store-mediated Ca2+ entry in mouse pancreatic acinar cells." Biochemical Journal 370, no. 1 (2003): 255–63. http://dx.doi.org/10.1042/bj20021505.

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Store-mediated Ca2+ entry (SMCE) is one of the main pathways for Ca2+ influx in non-excitable cells. Recent studies favour a secretion-like coupling mechanism to explain SMCE, where Ca2+ entry is mediated by an interaction of the endoplasmic reticulum (ER) with the plasma membrane (PM) and is modulated by the actin cytoskeleton. To explore this possibility further we have now investigated the role of the actin cytoskeleton in the activation and maintenance of SMCE in pancreatic acinar cells, a more specialized secretory cell type which might be an ideal cellular model to investigate further th

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29

Chinthalapudi, Krishna, Erumbi Rangarajan, Dipak Patil, and Tina Izard. "Lipid-directed cytoskeletal protein oligomerization at sites of cell adhesion." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1833. http://dx.doi.org/10.1107/s2053273314081674.

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Vertebrate cell growth, division, migration, morphogenesis, and development, rely on the dynamic interactions of cells with components the extracellular matrix (ECM) via cell surface complexes. These focal adhesions (FAs) are comprised of integrin receptors, associated signaling molecules, and talin, which is required for "inside-out" signaling that stabilizes contacts of integrin receptors with the ECM by linking FAs to the actin cytoskeleton by binding to vinculin. The highly dynamic interactions with the actin cytoskeleton are also essential for the formation of membrane protrusions (lamell

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30

Vafiadaki, Elizabeth, Demetrios A. Arvanitis, Aristides G. Eliopoulos, Evangelia G. Kranias, and Despina Sanoudou. "The Cardioprotective PKA-Mediated Hsp20 Phosphorylation Modulates Protein Associations Regulating Cytoskeletal Dynamics." International Journal of Molecular Sciences 21, no. 24 (2020): 9572. http://dx.doi.org/10.3390/ijms21249572.

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The cytoskeleton has a primary role in cardiomyocyte function, including the response to mechanical stimuli and injury. The small heat shock protein 20 (Hsp20) conveys protective effects in cardiac muscle that are linked to serine-16 (Ser16) Hsp20 phosphorylation by stress-induced PKA, but the link between Hsp20 and the cytoskeleton remains poorly understood. Herein, we demonstrate a physical and functional interaction of Hsp20 with the cytoskeletal protein 14-3-3. We show that, upon phosphorylation at Ser16, Hsp20 translocates from the cytosol to the cytoskeleton where it binds to 14-3-3. Thi

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31

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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32

Higuchi-Sanabria, Ryo, Joseph W. Paul, Jenni Durieux, et al. "Spatial regulation of the actin cytoskeleton by HSF-1 during aging." Molecular Biology of the Cell 29, no. 21 (2018): 2522–27. http://dx.doi.org/10.1091/mbc.e18-06-0362.

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There are many studies suggesting an age-associated decline in the actin cytoskeleton, and this has been adopted as common knowledge in the field of aging biology. However, a direct identification of this phenomenon in aging multicellular organisms has not been performed. Here, we express LifeAct::mRuby in a tissue-specific manner to interrogate cytoskeletal organization as a function of age. We show for the first time in Caenorhabditis elegans that the organization and morphology of the actin cytoskeleton deteriorate at advanced age in the muscles, intestine, and hypodermis. Moreover, hsf-1 i

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33

Lehtonen, Sanna, Fang Zhao, and Eero Lehtonen. "CD2-associated protein directly interacts with the actin cytoskeleton." American Journal of Physiology-Renal Physiology 283, no. 4 (2002): F734—F743. http://dx.doi.org/10.1152/ajprenal.00312.2001.

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CD2-associated protein (CD2AP) is an adapter protein associating with several membrane proteins, including nephrin, mutated in congenital nephrotic syndrome of the Finnish type, and polycystin-2, mutated in type 2 autosomal dominant polycystic kidney disease. Both proteins have critical roles in the maintenance of the integrity of the nephrons. Previous studies have suggested a role for CD2AP in the regulation of the organization of the actin cytoskeleton, but it has not been known whether the postulated association between CD2AP and actin is direct or mediated by other proteins. In this study

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34

Molitoris, B. A. "Putting the actin cytoskeleton into perspective: pathophysiology of ischemic alterations." American Journal of Physiology-Renal Physiology 272, no. 4 (1997): F430—F433. http://dx.doi.org/10.1152/ajprenal.1997.272.4.f430.

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The actin cytoskeleton plays an ever-increasingly understood role in mediating a myriad of processes necessary for cellular structure and function. New and exciting information regarding the dynamic aspects of the actin cytoskeleton and its intracellular regulation are unfolding at a rapid rate. Actin cytoskeletal-surface membrane interactions mediating such diverse cellular events as cell polarity, endocytosis, exocytosis, cell division, cellular migration, cell adhesion, signal transduction, and ion channel activity are part of an ever-growing list of cellular processes dependent on precise

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35

Fox, Joan E. B. "The Platelet Cytoskeleton." Thrombosis and Haemostasis 70, no. 06 (1993): 0884–93. http://dx.doi.org/10.1055/s-0038-1649694.

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SummaryThe platelet cytoskeleton contains two actin filament-based components. One is the cytoplasmic actin filaments which fill the cytoplasm and mediate contractile events. The other is the membrane skeleton, which coats the plasma membrane and regulates properties of the membrane such as its contours and stability. In the unstimulated platelet, only 30-40% of the actin is polymerized into filaments; the rest is thought to be prevented from polymerizing by the association of thymosin β4 with monomeric actin and by the association of gelsolin with the barbed ends of pre-existing actin filamen

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Wang, Jingyi, Na Lian, Yue Zhang, et al. "The Cytoskeleton in Plant Immunity: Dynamics, Regulation, and Function." International Journal of Molecular Sciences 23, no. 24 (2022): 15553. http://dx.doi.org/10.3390/ijms232415553.

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The plant cytoskeleton, consisting of actin filaments and microtubules, is a highly dynamic filamentous framework involved in plant growth, development, and stress responses. Recently, research has demonstrated that the plant cytoskeleton undergoes rapid remodeling upon sensing pathogen attacks, coordinating the formation of microdomain immune complexes, the dynamic and turnover of pattern-recognizing receptors (PRRs), the movement and aggregation of organelles, and the transportation of defense compounds, thus serving as an important platform for responding to pathogen infections. Meanwhile,

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Edmonds, B. T., J. Wyckoff, Y. G. Yeung, et al. "Elongation factor-1 alpha is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma." Journal of Cell Science 109, no. 11 (1996): 2705–14. http://dx.doi.org/10.1242/jcs.109.11.2705.

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Overexpression of elongation factor-1 alpha (EF1 alpha) mRNA has been correlated with increased metastatic potential in mammary adenocarcinoma; however, this relationship was not explored at the level of protein expression. As EF1 alpha has been shown in other cell types to be a component of the actin cytoskeleton, a likely effector in metastasis, the actin binding activity of EF1 alpha from metastatic and nonmetastatic rat breast tumors and cell lines was investigated. We have shown that EF1 alpha protein is overexpressed in metastatic compared to nonmetastatic cells and whole tumors. Similar

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Flaumenhaft, Robert, James R. Dilks, Nataliya Rozenvayn та Kamil Woronowicz. "The Platelet Actin Cytoskeleton Associates Directly with Syntaxin-4 and Participates in α-Granule Secretion." Blood 112, № 11 (2008): 1839. http://dx.doi.org/10.1182/blood.v112.11.1839.1839.

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Abstract Following platelet activation, platelets undergo a dramatic shape change directed by the actin cytoskeleton and accompanied by secretion of granule contents. Secretion of platelet granules requires soluble NSF Attachment Protein Receptors (SNAREs) that mediate fusion events required for granule release. While the actin cytoskeleton is thought to influence platelet granule secretion, the mechanism of this influence is not known. We sought to determine whether actin controls α-granule release by interacting with platelet SNAREs. We found that disruption of the actin cytoskeleton by latr

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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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Kamińska, Joanna, Beata Gajewska, Anita K. Hopper, and Teresa ˙Zołądek. "Rsp5p, a New Link between the Actin Cytoskeleton and Endocytosis in the Yeast Saccharomyces cerevisiae." Molecular and Cellular Biology 22, no. 20 (2002): 6946–48. http://dx.doi.org/10.1128/mcb.22.20.6946-6958.2002.

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ABSTRACT Rsp5p is an ubiquitin-protein ligase of Saccharomyces cerevisiae that has been implicated in numerous processes including transcription, mitochondrial inheritance, and endocytosis. Rsp5p functions at multiple steps of endocytosis, including ubiquitination of substrates and other undefined steps. We propose that one of the roles of Rsp5p in endocytosis involves maintenance and remodeling of the actin cytoskeleton. We report the following. (i) There are genetic interactions between rsp5 and several mutant genes encoding actin cytoskeletal proteins. rsp5 arp2, rsp5 end3, and rsp5 sla2 do

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Vlahovich, Nicole, Anthony J. Kee, Chris Van der Poel, et al. "Cytoskeletal Tropomyosin Tm5NM1 Is Required for Normal Excitation–Contraction Coupling in Skeletal Muscle." Molecular Biology of the Cell 20, no. 1 (2009): 400–409. http://dx.doi.org/10.1091/mbc.e08-06-0616.

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The functional diversity of the actin microfilaments relies in part on the actin binding protein tropomyosin (Tm). The muscle-specific Tms regulate actin-myosin interactions and hence contraction. However, there is less known about the roles of the numerous cytoskeletal isoforms. We have shown previously that a cytoskeletal Tm, Tm5NM1, defines a Z-line adjacent cytoskeleton in skeletal muscle. Recently, we identified a second cytoskeletal Tm in this region, Tm4. Here we show that Tm4 and Tm5NM1 define separate actin filaments; the former associated with the terminal sarcoplasmic reticulum (SR)

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Gonzalez-Quevedo, Rosa, Marina Shoffer, Lily Horng, and Anthony E. Oro. "Receptor tyrosine phosphatase–dependent cytoskeletal remodeling by the hedgehog-responsive gene MIM/BEG4." Journal of Cell Biology 168, no. 3 (2005): 453–63. http://dx.doi.org/10.1083/jcb.200409078.

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During development, dynamic remodeling of the actin cytoskeleton allows the precise placement and morphology of tissues. Morphogens such as Sonic hedgehog (Shh) and local cues such as receptor protein tyrosine phosphatases (RPTPs) mediate this process, but how they regulate the cytoskeleton is poorly understood. We previously identified Basal cell carcinoma–enriched gene 4 (BEG4)/Missing in Metastasis (MIM), a Shh-inducible, Wiskott-Aldrich homology 2 domain–containing protein that potentiates Gli transcription (Callahan, C.A., T. Ofstad, L. Horng, J.K. Wang, H.H. Zhen, P.A. Coulombe, and A.E.

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Liu, Yi, Keyvan Mollaeian, Muhammad Huzaifah Shamim, and Juan Ren. "Effect of F-actin and Microtubules on Cellular Mechanical Behavior Studied Using Atomic Force Microscope and an Image Recognition-Based Cytoskeleton Quantification Approach." International Journal of Molecular Sciences 21, no. 2 (2020): 392. http://dx.doi.org/10.3390/ijms21020392.

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Cytoskeleton morphology plays a key role in regulating cell mechanics. Particularly, cellular mechanical properties are directly regulated by the highly cross-linked and dynamic cytoskeletal structure of F-actin and microtubules presented in the cytoplasm. Although great efforts have been devoted to investigating the qualitative relation between the cellular cytoskeleton state and cell mechanical properties, comprehensive quantification results of how the states of F-actin and microtubules affect mechanical behavior are still lacking. In this study, the effect of both F-actin and microtubules

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Chia, C. P., I. Khrebtukova, J. McCluskey, and W. F. Wade. "MHC class II molecules that lack cytoplasmic domains are associated with the cytoskeleton." Journal of Immunology 153, no. 8 (1994): 3398–407. http://dx.doi.org/10.4049/jimmunol.153.8.3398.

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Abstract MHC class II molecules, composed of alpha- and beta-chain heterodimers, are required for Ag presentation. The carboxyl-terminal domains of class II molecules are believed to mediate the location of class II in the plasma membrane and are important for signal transduction and Ag presentation. These domains contain typical transmembrane sequences, and cytoplasmic sequences of 12 or 18 amino acids for the alpha- and beta-chains, respectively. We examined these domains to determine whether they linked class II molecules to the actin-based cytoskeleton. Our analyses of class II-cytoskeleto

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Sousa, Vítor L., Serena Bellani, Maila Giannandrea та ін. "α-Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics". Molecular Biology of the Cell 20, № 16 (2009): 3725–39. http://dx.doi.org/10.1091/mbc.e08-03-0302.

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The function of α-synuclein, a soluble protein abundant in the brain and concentrated at presynaptic terminals, is still undefined. Yet, α-synuclein overexpression and the expression of its A30P mutant are associated with familial Parkinson's disease. Working in cell-free conditions, in two cell lines as well as in primary neurons we demonstrate that α-synuclein and its A30P mutant have different effects on actin polymerization. Wild-type α-synuclein binds actin, slows down its polymerization and accelerates its depolymerization, probably by monomer sequestration; A30P mutant α-synuclein incre

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López-Contreras, L., V. I. Hernández-Ramírez, A. E. Lagunes-Guillén, et al. "Exploring the Possible Role of Lysine Acetylation onEntamoeba histolyticaVirulence: A Focus on the Dynamics of the Actin Cytoskeleton." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/757392.

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Cytoskeleton remodeling can be regulated, among other mechanisms, by lysine acetylation. The role of acetylation on cytoskeletal and other proteins ofEntamoeba histolyticahas been poorly studied. Dynamic rearrangements of the actin cytoskeleton are crucial for amebic motility and capping formation, processes that may be effective means of evading the host immune response. Here we report the possible effect of acetylation on the actin cytoskeleton dynamics andin vivovirulence ofE. histolytica. Using western blot, immunoprecipitation, microscopy assays, andin silicoanalysis, we show results that

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Vu, Vivian, Phuong Bui, Megumi Eguchi, Aimin Xu, and Gary Sweeney. "Globular adiponectin induces LKB1/AMPK-dependent glucose uptake via actin cytoskeleton remodeling." Journal of Molecular Endocrinology 51, no. 1 (2013): 155–65. http://dx.doi.org/10.1530/jme-13-0059.

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Previous studies have shown that many metabolic actions of adiponectin are mediated via the activation of AMP kinase and that adiponectin stimulates GLUT4 translocation and glucose uptake in the muscle. In this study, we demonstrate that adiponectin stimulates actin cytoskeleton remodeling, with increased phosphorylation of cofilin, and that blocking of cytoskeletal remodeling with cytochalasin D prevents adiponectin-stimulated AMPK phosphorylation in L6 myoblasts. LKB1 is an upstream kinase of AMPK, and we observed the colocalization of LKB1 with filamentous actin in response to adiponectin.

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Wender, Nomy, Eduardo Villalobo, and David Mirelman. "EhLimA, a Novel LIM Protein, Localizes to the Plasma Membrane in Entamoeba histolytica." Eukaryotic Cell 6, no. 9 (2007): 1646–55. http://dx.doi.org/10.1128/ec.00177-07.

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ABSTRACT The parasitic protozoan Entamoeba histolytica relies on a very dynamic cytoskeleton in order to invade and survive in host tissues. Identification of cytoskeletal elements is key to understanding these processes. Here we present the characterization of EhLimA, the first LIM protein of E. histolytica. EhLimA consists of a single LIM domain at its N terminus and exhibits the highest degree of homology with DdLimE from Dictyostelium discoideum. Immunofluorescence localization of EhLimA using anti-EhLimA antibodies revealed that EhLimA is highly concentrated at the plasma membrane of cell

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Wu, Ru Feng, Ying Gu, You Cheng Xu, Stefania Mitola, Federico Bussolino, and Lance S. Terada. "Human Immunodeficiency Virus Type 1 Tat Regulates Endothelial Cell Actin Cytoskeletal Dynamics through PAK1 Activation and Oxidant Production." Journal of Virology 78, no. 2 (2004): 779–89. http://dx.doi.org/10.1128/jvi.78.2.779-789.2004.

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ABSTRACT Human immunodeficiency virus type 1 Tat exerts prominent angiogenic effects which may lead to a variety of vasculopathic conditions in AIDS patients. Because endothelial cells undergo prominent cytoskeletal rearrangement during angiogenesis, we investigated the specific effects of Tat on the endothelial cell actin cytoskeleton. Glutathione S-transferase (GST)-Tat, at a level of 200 ng/ml (equivalent to 52 ng of Tat/ml), caused stress fiber disassembly, peripheral retraction, and ruffle formation in human umbilical vein endothelial cells (HUVEC) and human lung microvascular endothelial

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Zhao, Yongtong, Sandor S. Shapiro, and Masumi Eto. "F-actin clustering and cell dysmotility induced by the pathological W148R missense mutation of filamin B at the actin-binding domain." American Journal of Physiology-Cell Physiology 310, no. 1 (2016): C89—C98. http://dx.doi.org/10.1152/ajpcell.00274.2015.

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Filamin B (FLNB) is a dimeric actin-binding protein that orchestrates the reorganization of the actin cytoskeleton. Congenital mutations of FLNB at the actin-binding domain (ABD) are known to cause abnormalities of skeletal development, such as atelosteogenesis types I and III and Larsen's syndrome, although the underlying mechanisms are poorly understood. Here, using fluorescence microscopy, we characterized the reorganization of the actin cytoskeleton in cells expressing each of six pathological FLNB mutants that have been linked to skeletal abnormalities. The subfractionation assay showed a

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