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Artykuły w czasopismach na temat „Cytoskeleton”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 lipca 2025

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1

Smith, CM, SM Burris, GH Rao, and JG White. "Detergent-resistant cytoskeleton of the surface-activated platelet differs from the suspension-activated platelet cytoskeleton." Blood 80, no. 11 (1992): 2774–80. http://dx.doi.org/10.1182/blood.v80.11.2774.2774.

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Abstract This study contrasts the protein composition of the detergent-resistant cytoskeleton of platelets fully spread on glass with the cytoskeletal composition of resting platelets and platelets aggregated in suspension with thrombin. Complete Triton X-100-insoluble cytoskeletons were isolated from spread, resting, and suspension-activated platelets in the presence of protease inhibitors, solubilized in sodium dodecyl sulfate/EDTA and analyzed on reduced, one-dimensional polyacrylamide gels. The protein composition of the cytoskeletons differed both qualitatively and quantitatively. Most no

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Smith, CM, SM Burris, GH Rao, and JG White. "Detergent-resistant cytoskeleton of the surface-activated platelet differs from the suspension-activated platelet cytoskeleton." Blood 80, no. 11 (1992): 2774–80. http://dx.doi.org/10.1182/blood.v80.11.2774.bloodjournal80112774.

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This study contrasts the protein composition of the detergent-resistant cytoskeleton of platelets fully spread on glass with the cytoskeletal composition of resting platelets and platelets aggregated in suspension with thrombin. Complete Triton X-100-insoluble cytoskeletons were isolated from spread, resting, and suspension-activated platelets in the presence of protease inhibitors, solubilized in sodium dodecyl sulfate/EDTA and analyzed on reduced, one-dimensional polyacrylamide gels. The protein composition of the cytoskeletons differed both qualitatively and quantitatively. Most notable wer

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3

Wiegant, F. A., F. J. Blok, L. H. Defize, W. A. Linnemans, A. J. Verkley, and J. Boonstra. "Epidermal growth factor receptors associated to cytoskeletal elements of epidermoid carcinoma (A431) cells." Journal of Cell Biology 103, no. 1 (1986): 87–94. http://dx.doi.org/10.1083/jcb.103.1.87.

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The structural interaction of the epidermal growth factor (EGF) receptor and the cytoskeleton of A431 cells has been studied using a monoclonal anti-EGF receptor antibody. This has been done with immunogold labeling using a variety of electron microscopical preparation procedures and EGF binding studies. By providing an image of the membrane-associated cytoskeleton, the dry cleavage method reveals a preferential localization of EGF receptors superimposed upon cytoskeletal filaments. The colocalization of gold particles with cytoskeletal filaments is not affected when pre-labeled cells are extr

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4

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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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

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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7

Wickstead, Bill, and Keith Gull. "The evolution of the cytoskeleton." Journal of Cell Biology 194, no. 4 (2011): 513–25. http://dx.doi.org/10.1083/jcb.201102065.

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The cytoskeleton is a system of intracellular filaments crucial for cell shape, division, and function in all three domains of life. The simple cytoskeletons of prokaryotes show surprising plasticity in composition, with none of the core filament-forming proteins conserved in all lineages. In contrast, eukaryotic cytoskeletal function has been hugely elaborated by the addition of accessory proteins and extensive gene duplication and specialization. Much of this complexity evolved before the last common ancestor of eukaryotes. The distribution of cytoskeletal filaments puts constraints on the l

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8

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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9

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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10

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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11

Mecham, J. O., M. M. Soong, C. A. Cain, S. Koehm, J. Goff, and W. A. Tompkins. "Binding of calmodulin to the microfilament network correlates with induction of a macrophage tumoricidal response." Journal of Immunology 134, no. 5 (1985): 3516–23. http://dx.doi.org/10.4049/jimmunol.134.5.3516.

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Abstract Induction of mouse peritoneal macrophage cytotoxicity against SV3T3, a line of virally transformed mouse cells correlated with the distribution of cytoplasmic calmodulin in the macrophages. The organization of the cytoskeleton was examined by fluorescent microscopy and by transmission electron microscopy, using immunogold tagging after Triton-X-100 (TX-100) extraction of the macrophages. Macrophages that had been activated to a tumoricidal state in vivo by vaccinia virus or in vitro by lymphokine stimulation displayed cytoskeletal networks that were more extended and weblike than did

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12

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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13

Geisterfer, Zachary M., Gabriel Guilloux, Jesse C. Gatlin, and Romain Gibeaux. "The Cytoskeleton and Its Roles in Self-Organization Phenomena: Insights from Xenopus Egg Extracts." Cells 10, no. 9 (2021): 2197. http://dx.doi.org/10.3390/cells10092197.

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Self-organization of and by the cytoskeleton is central to the biology of the cell. Since their introduction in the early 1980s, cytoplasmic extracts derived from the eggs of the African clawed-frog, Xenopus laevis, have flourished as a major experimental system to study the various facets of cytoskeleton-dependent self-organization. Over the years, the many investigations that have used these extracts uniquely benefited from their simplified cell cycle, large experimental volumes, biochemical tractability and cell-free nature. Here, we review the contributions of egg extracts to our understan

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14

Toyoda, Hideki, Keiji Nakai, Serdar B. Omay, et al. "Differential Association of Protein Ser/Thr Phosphatase Types 1 and 2A with the Cytoskeleton upon Platelet Activation." Thrombosis and Haemostasis 76, no. 06 (1996): 1053–62. http://dx.doi.org/10.1055/s-0038-1650706.

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SummaryThe association of protein Ser/Thr phosphatase type 1(PP1) and type 2A (PP2A) with the cytoskeleton (Triton X-100 insoluble residue) during human platelet activation was investigated. In unstimulated platelets, 40% of total PPl-like activity was present in the Triton-insoluble cytoskeleton, while only 10% of the total PP2A-like activity was present in this fraction. Stimulation with 1 U/ml thrombin produced a 1.8-fold increase in PPl-like activity and a 7-fold increase in PP2A-like activity, respectively, in the cytoskeletal fraction, under aggregating conditions. Immunoblot analysis re

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15

Chen, Jing, and Mark C. Wagner. "Altered membrane-cytoskeleton linkage and membrane blebbing in energy-depleted renal proximal tubular cells." American Journal of Physiology-Renal Physiology 280, no. 4 (2001): F619—F627. http://dx.doi.org/10.1152/ajprenal.2001.280.4.f619.

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The effects of energy depletion on two membrane-cytoskeletal linker proteins (ezrin and myosin-1β) and membrane bleb formation were studied in isolated rabbit proximal tubule cells. Measurements of cytoskeletal-membrane interactions by using the laser optic trap method revealed a stronger association of control tubule membrane with the apical cytoskeleton compared with the basal cytoskeleton. Energy depletion weakened the apical membrane-cytoskeleton interactions to a greater degree. Biochemical studies demonstrated that energy depletion altered both ezrin and myosin-1β. The salt-insensitive e

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16

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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17

Snapp, Erik L., and Scott M. Landfear. "Cytoskeletal Association Is Important for Differential Targeting of Glucose Transporter Isoforms in Leishmania." Journal of Cell Biology 139, no. 7 (1997): 1775–83. http://dx.doi.org/10.1083/jcb.139.7.1775.

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The major glucose transporter of the parasitic protozoan Leishmania enriettii exists in two isoforms, one of which (iso-1) localizes to the flagellar membrane, while the other (iso-2) localizes to the plasma membrane of the cell body, the pellicular membrane. These two isoforms differ only in their cytosolic NH2-terminal domains. Using immunoblots and immunofluorescence microscopy of detergent-extracted cytoskeletons, we have demonstrated that iso-2 associates with the microtubular cytoskeleton that underlies the cell body membrane, whereas the flagellar membrane isoform iso-1 does not associa

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18

Patton, W. F., M. R. Dhanak, and B. S. Jacobson. "Differential partitioning of plasma membrane proteins into the triton X-100-insoluble cytoskeleton fraction during concanavalin A-induced receptor redistribution." Journal of Cell Science 92, no. 1 (1989): 85–91. http://dx.doi.org/10.1242/jcs.92.1.85.

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The plasma membrane proteins of Dictyostelium discoideum were characterized with respect to their partitioning into the Triton-insoluble cytoskeleton fraction of the cell during concanavalin A-induced capping. Two fractions of plasma membrane-associated concanavalin A were identified; one that immediately associated with the cytoskeleton fraction via cell surface glycoproteins, and one that partitioned with the cytoskeleton only after extensive cell surface glycoprotein cross-linking. Three major classes of polypeptides were found in the plasma membrane that differed with respect to their part

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19

Madara, J. L. "Intestinal absorptive cell tight junctions are linked to cytoskeleton." American Journal of Physiology-Cell Physiology 253, no. 1 (1987): C171—C175. http://dx.doi.org/10.1152/ajpcell.1987.253.1.c171.

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Permeation of intercellular tight junctions in epithelia may be altered by maneuvers that affect the cytoskeleton. Conversely, agents that alter tight-junction permeability also often produce alterations in cytoskeletal structure. However, anatomic links between the tight junction and the cytoskeleton have not been clearly defined. We explore the anatomy of the perijunctional cytoskeleton by applying electron microscopy to cytoskeletal preparations of whole intestinal absorptive cells using detergent extraction techniques. Individual elements of the perijunctional cytoskeleton, including actin

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Bruin, Taco, Guus M. Asijee, Arie Prins, Jan Wouter ten Cate, and Augueste Sturk. "Subcellular Distribution and Phosphorylation of Vinculin lsoforms in Human Blood Platelets." Thrombosis and Haemostasis 65, no. 02 (1991): 206–11. http://dx.doi.org/10.1055/s-0038-1647485.

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SummaryIn this study we investigated human blood platelet vinculin microheterogeneity, the subcellular localization and phosphorylation of the different isoforrns before and after platelet stimulation. At least 5 vinculin isoforms could be detected, as well as metavinculin. These isofonns did not demonstrate a specific subcellular localization, i. e. their relative content was similar in cytoskeleton, membrane skeleton and cytosol. Upon platelet stimulation with thrombin a small increase in α’-vinculin was noted in all platelet subfractions. The cytoskeleton of non-stimulated platelets contain

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Mirvis, Mary, Tim Stearns, and W. James Nelson. "Cilium structure, assembly, and disassembly regulated by the cytoskeleton." Biochemical Journal 475, no. 14 (2018): 2329–53. http://dx.doi.org/10.1042/bcj20170453.

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The cilium, once considered a vestigial structure, is a conserved, microtubule-based organelle critical for transducing extracellular chemical and mechanical signals that control cell polarity, differentiation, and proliferation. The cilium undergoes cycles of assembly and disassembly that are controlled by complex inter-relationships with the cytoskeleton. Microtubules form the core of the cilium, the axoneme, and are regulated by post-translational modifications, associated proteins, and microtubule dynamics. Although actin and septin cytoskeletons are not major components of the axoneme, th

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Joshi, Divyesh, and Maneesha S. Inamdar. "Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling." Molecular Biology of the Cell 30, no. 12 (2019): 1437–50. http://dx.doi.org/10.1091/mbc.e18-08-0484.

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Blood vessel formation requires endothelial cell (EC) migration that depends on dynamic remodeling of the cytoskeleton. Rudhira/Breast Carcinoma Amplified Sequence 3 (BCAS3) is a cytoskeletal protein essential for EC migration and sprouting angiogenesis during mouse development and is implicated in metastatic disease. Here, we report that Rudhira mediates cytoskeleton organization and dynamics during EC migration. Rudhira binds to both microtubules (MTs) and vimentin intermediate filaments (IFs) and stabilizes MTs. Rudhira depletion impairs cytoskeletal cross-talk, MT stability, and hence foca

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Kucik, Dennis F., Timothy E. O'Toole, Alexander Zheleznyak, Denise K. Busettini та Eric J. Brown. "Activation-enhanced αIIbβ3-Integrin–Cytoskeleton Interactions Outside of Focal Contacts Require the α-Subunit". Molecular Biology of the Cell 12, № 5 (2001): 1509–18. http://dx.doi.org/10.1091/mbc.12.5.1509.

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Integrins link the cell's cytoskeleton to the extracellular matrix, as well as to receptors on other cells. These links occur not only at focal contacts but also at smaller integrin-containing protein complexes outside of focal contacts. We previously demonstrated the importance of focal contact-independent integrin–cytoskeleton interactions of β2 integrins: activation of adhesion resulted from a release of integrins from cytoskeletal constraints. To determine whether changes in integrin–cytoskeleton interactions were related to activation of the integrin, we used single particle tracking to e

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Peerschke, EI. "Time-dependent association between platelet-bound fibrinogen and the Triton X-100 insoluble cytoskeleton." Blood 77, no. 3 (1991): 508–14. http://dx.doi.org/10.1182/blood.v77.3.508.508.

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Abstract Previous studies indicated a correlation between the formation of EDTA- resistant (irreversible) platelet-fibrinogen interactions and platelet cytoskeleton formation. The present study explored the direct association of membrane-bound fibrinogen with the Triton X-100 (Sigma Chemical Co, St Louis, MO) insoluble cytoskeleton of aspirin-treated, gel-filtered platelets, activated but not aggregated with 20 mumol/L adenosine diphosphate (ADP) or 150 mU/mL human thrombin (THR) when bound fibrinogen had become resistant to dissociation by EDTA. Conversion of exogenous 125I-fibrinogen to fibr

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Peerschke, EI. "Time-dependent association between platelet-bound fibrinogen and the Triton X-100 insoluble cytoskeleton." Blood 77, no. 3 (1991): 508–14. http://dx.doi.org/10.1182/blood.v77.3.508.bloodjournal773508.

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Previous studies indicated a correlation between the formation of EDTA- resistant (irreversible) platelet-fibrinogen interactions and platelet cytoskeleton formation. The present study explored the direct association of membrane-bound fibrinogen with the Triton X-100 (Sigma Chemical Co, St Louis, MO) insoluble cytoskeleton of aspirin-treated, gel-filtered platelets, activated but not aggregated with 20 mumol/L adenosine diphosphate (ADP) or 150 mU/mL human thrombin (THR) when bound fibrinogen had become resistant to dissociation by EDTA. Conversion of exogenous 125I-fibrinogen to fibrin was pr

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Geppert, T. D., and P. E. Lipsky. "Association of various T cell-surface molecules with the cytoskeleton. Effect of cross-linking and activation." Journal of Immunology 146, no. 10 (1991): 3298–305. http://dx.doi.org/10.4049/jimmunol.146.10.3298.

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Abstract The association of various surface molecules with the cytoskeleton in resting peripheral blood T cells was examined by assaying the capacity of detergent to solubilize them. Cytoskeletal association was assessed by staining T cells with a fluorescein-conjugated mAb, resuspending the cells in buffer with or without the nonionic detergent, NP-40, and determining the capacity of the detergent to remove the mAb from the cell surface by using flow microfluorimetry. MAb to CD3, the TCR, and CD45 were completely removed from the cell surface by detergent. In contrast, 7 to 50% of mAb to CD2,

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Woodward, R., M. J. Carden, and K. Gull. "Immunological characterization of cytoskeletal proteins associated with the basal body, axoneme and flagellum attachment zone of Trypanosoma brucei." Parasitology 111, no. 1 (1995): 77–85. http://dx.doi.org/10.1017/s0031182000064623.

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SUMMARYThe monoclonal antibody BS7, raised to bovine sperm flagellum cytoskeletal antigens in a previous study, is here reported to detect flagellum-associated structures in Trypanosoma brucei and Crithidia fasciculata. Immunoblotting showed that BS7 cross-reacts with several cytoskeletal T. brucei proteins but phosphatase treatment did not diminish this complex immunoblot reactivity. To characterize further the cross-reactive proteins recognized in T. brucei-cytoskeletons by BS7 each was excised from preparative gels and used as an immunogen for antiserum production. Two proteins, with appare

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Wiegand, Tina, and Anthony A. Hyman. "Drops and fibers — how biomolecular condensates and cytoskeletal filaments influence each other." Emerging Topics in Life Sciences 4, no. 3 (2020): 247–61. http://dx.doi.org/10.1042/etls20190174.

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The cellular cytoskeleton self-organizes by specific monomer–monomer interactions resulting in the polymerization of filaments. While we have long thought about the role of polymerization in cytoskeleton formation, we have only begun to consider the role of condensation in cytoskeletal organization. In this review, we highlight how the interplay between polymerization and condensation leads to the formation of the cytoskeleton.

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Ali, Moustafa R. K., Yue Wu, Yan Tang, et al. "Targeting cancer cell integrins using gold nanorods in photothermal therapy inhibits migration through affecting cytoskeletal proteins." Proceedings of the National Academy of Sciences 114, no. 28 (2017): E5655—E5663. http://dx.doi.org/10.1073/pnas.1703151114.

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Metastasis is responsible for most cancer-related deaths, but the current clinical treatments are not effective. Recently, gold nanoparticles (AuNPs) were discovered to inhibit cancer cell migration and prevent metastasis. Rationally designed AuNPs could greatly benefit their antimigration property, but the molecular mechanisms need to be explored. Cytoskeletons are cell structural proteins that closely relate to migration, and surface receptor integrins play critical roles in controlling the organization of cytoskeletons. Herein, we developed a strategy to inhibit cancer cell migration by tar

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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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Landreth, G. E., L. K. Williams, and G. D. Rieser. "Association of the epidermal growth factor receptor kinase with the detergent-insoluble cytoskeleton of A431 cells." Journal of Cell Biology 101, no. 4 (1985): 1341–50. http://dx.doi.org/10.1083/jcb.101.4.1341.

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The epidermal growth factor receptor (EGF-R) on human epidermoid carcinoma cells, A431, was found to be predominantly associated with the detergent-insoluble cytoskeleton, where it retained both a functional ligand-binding domain and an intrinsic tyrosine kinase activity. The EGF-R was constitutively associated with the A431 cytoskeleton; this association was not a consequence of adventitious binding. The EGF-R was associated with cytoskeletal elements both at the cell surface, within intracellular vesicles mediating the internalization of the hormone-receptor complex, and within lysosomes. Th

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García-Padilla, Carlos, María del Mar Muñoz-Gallardo, Estefanía Lozano-Velasco, et al. "New Insights into the Roles of lncRNAs as Modulators of Cytoskeleton Architecture and Their Implications in Cellular Homeostasis and in Tumorigenesis." Non-Coding RNA 8, no. 2 (2022): 28. http://dx.doi.org/10.3390/ncrna8020028.

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The importance of the cytoskeleton not only in cell architecture but also as a pivotal element in the transduction of signals that mediate multiple biological processes has recently been highlighted. Broadly, the cytoskeleton consists of three types of structural proteins: (1) actin filaments, involved in establishing and maintaining cell shape and movement; (2) microtubules, necessary to support the different organelles and distribution of chromosomes during cell cycle; and (3) intermediate filaments, which have a mainly structural function showing specificity for the cell type where they are

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Hutchings, Nathan R., John E. Donelson, and Kent L. Hill. "Trypanin is a cytoskeletal linker protein and is required for cell motility in African trypanosomes." Journal of Cell Biology 156, no. 5 (2002): 867–77. http://dx.doi.org/10.1083/jcb.200201036.

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The cytoskeleton of eukaryotic cells is comprised of a complex network of distinct but interconnected filament systems that function in cell division, cell motility, and subcellular trafficking of proteins and organelles. A gap in our understanding of this dynamic network is the identification of proteins that connect subsets of cytoskeletal structures. We previously discovered a family of cytoskeleton-associated proteins that includes GAS11, a candidate human tumor suppressor upregulated in growth-arrested cells, and trypanin, a component of the flagellar cytoskeleton of African trypanosomes.

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Jackson, Wesley M., Michael J. Jaasma, Raymond Y. Tang, and Tony M. Keaveny. "Mechanical loading by fluid shear is sufficient to alter the cytoskeletal composition of osteoblastic cells." American Journal of Physiology-Cell Physiology 295, no. 4 (2008): C1007—C1015. http://dx.doi.org/10.1152/ajpcell.00509.2007.

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Many structural modifications have been observed as a part of the cellular response to mechanical loading in a variety of cell types. Although changes in morphology and cytoskeletal rearrangement have been widely reported, few studies have investigated the change in cytoskeletal composition. Measuring how the amounts of specific structural proteins in the cytoskeleton change in response to mechanical loading will help to elucidate cellular mechanisms of functional adaptation to the applied forces. Therefore, the overall hypothesis of this study was that osteoblasts would respond to fluid shear

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Resch, Guenter P., Kenneth N. Goldie, Angelika Krebs, Andreas Hoenger, and J. Victor Small. "Visualisation of the actin cytoskeleton by cryo-electron microscopy." Journal of Cell Science 115, no. 9 (2002): 1877–82. http://dx.doi.org/10.1242/jcs.115.9.1877.

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An understanding of the mechanisms driving cell motility requires clarification of the structural organisation of actin filament arrays in the regions of cell protrusion termed lamellipodia. Currently, there is a lack of consensus on lamellipodia organisation stemming from the application of alternative procedures for ultrastructural visualisation of cytoskeleton networks. In this study, we show that cryo-electron microscopy of extracted cytoskeletons embedded in a thin layer of vitreous ice can reveal the organisation of cytoskeletal elements at high resolution. Since this method involves no

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Kuhn, J. R., and M. Poenie. "Modulated polarization microscopy displays the dynamics of cytoskeletal structures in living, motile cells." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 902–3. http://dx.doi.org/10.1017/s0424820100140889.

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Cell shape and movement are controlled by elements of the cytoskeleton including actin filaments an microtubules. Unfortunately, it is difficult to visualize the cytoskeleton in living cells and hence follow it dynamics. Immunofluorescence and ultrastructural studies of fixed cells while providing clear images of the cytoskeleton, give only a static picture of this dynamic structure. Microinjection of fluorescently Is beled cytoskeletal proteins has proved useful as a way to follow some cytoskeletal events, but long terry studies are generally limited by the bleaching of fluorophores and prese

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Lee, Kyu Joon, Qing Zhou та Ziyin Li. "CRK2 controls cytoskeleton morphogenesis in Trypanosoma brucei by phosphorylating β-tubulin to regulate microtubule dynamics". PLOS Pathogens 19, № 3 (2023): e1011270. http://dx.doi.org/10.1371/journal.ppat.1011270.

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Microtubules constitute a vital part of the cytoskeleton in eukaryotes by mediating cell morphogenesis, cell motility, cell division, and intracellular transport. The cytoskeleton of the parasite Trypanosoma brucei contains an array of subpellicular microtubules with their plus-ends positioned toward the posterior cell tip, where extensive microtubule growth and cytoskeleton remodeling take place during early cell cycle stages. However, the control mechanism underlying microtubule dynamics at the posterior cell tip remains elusive. Here, we report that the S-phase cyclin-dependent kinase-cycli

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Kost, Benedikt, Yi-Qun Bao, and Nam-Hai Chua. "Cytoskeleton and plant organogenesis." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1422 (2002): 777–89. http://dx.doi.org/10.1098/rstb.2002.1090.

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The functions of microtubules and actin filaments during various processes that are essential for the growth, reproduction and survival of single plant cells have been well characterized. A large number of plant structural cytoskeletal or cytoskeleton–associated proteins, as well as genes encoding such proteins, have been identified. Although many of these genes and proteins have been partially characterized with respect to their functions, a coherent picture of how they interact to execute cytoskeletal functions in plant cells has yet to emerge. Cytoskeleton–controlled cellular processes are

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Foo, Kar Yue, and Hui-Yee Chee. "Interaction betweenFlavivirusand Cytoskeleton during Virus Replication." BioMed Research International 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/427814.

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Flaviviruses are potentially human pathogens that cause major epidemics worldwide.Flavivirusinteracts with host cell factors to form a favourable virus replication site. Cell cytoskeletons have been observed to have close contact with flaviviruses, which expands the understanding of cytoskeleton functions during virus replication, although many detailed mechanisms are still unclear. The interactions between the virus and host cytoskeletons such as actin filaments, microtubules, and intermediate filaments have provided insight into molecular alterations during the virus infection, such as viral

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Karavashkova, Olga, Artem Minin, Alexandra Maltseva, et al. "Effect of a Constant Magnetic Field on Cell Morphology and Migration Mediated by Cytoskeleton-Bound Magnetic Nanoparticles." International Journal of Molecular Sciences 26, no. 11 (2025): 5330. https://doi.org/10.3390/ijms26115330.

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Cell migration, shape maintenance, and intracellular signaling are closely linked to dynamic changes in cell morphology and the cytoskeleton. These processes involve the reorganization of the cytoskeleton within the cytoplasm, affecting all its key components: intermediate filaments, microtubules, and microfilaments. A promising strategy for remotely controlling cellular functions is the use of magnetic nanoparticles, which can influence cellular physiology. This approach, known as magnetogenetics, has been applied in various areas of cell and molecular biology. Applying a magnetic field allow

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Gao, Ya-sheng, and Elizabeth Sztul. "A Novel Interaction of the Golgi Complex with the Vimentin Intermediate Filament Cytoskeleton." Journal of Cell Biology 152, no. 5 (2001): 877–94. http://dx.doi.org/10.1083/jcb.152.5.877.

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The integration of the vimentin intermediate filament (IF) cytoskeleton and cellular organelles in vivo is an incompletely understood process, and the identities of proteins participating in such events are largely unknown. Here, we show that the Golgi complex interacts with the vimentin IF cytoskeleton, and that the Golgi protein formiminotransferase cyclodeaminase (FTCD) participates in this interaction. We show that the peripherally associated Golgi protein FTCD binds directly to vimentin subunits and to polymerized vimentin filaments in vivo and in vitro. Expression of FTCD in cultured cel

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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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Symington, Alison L., Selma Zimmerman, and A. M. Zimmerman. "The influence of hydrostatic pressure on the distribution of histone mRNA in HeLa cells." Biochemistry and Cell Biology 71, no. 3-4 (1993): 150–55. http://dx.doi.org/10.1139/o93-024.

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Hydrostatic pressure and HeLa S3 cells were used (as a model system) to investigate the relationship of the cytoskeleton and histone gene expression. Exposure of HeLa S3 cells to hydrostatic pressure of 1000 – 10 000 psi (6.89 × 103 – 6.89 × 104 kPa) disrupts the cytoskeleton and reduces H1 and core histone mRNA and actin mRNA levels as determined by hybridization to specific DNA probes. Soluble and insoluble cell fractions were isolated from HeLa cells after lysis in Triton X-100 buffered with PIPES and being subjected to low-speed centrifugation. The insoluble fraction was designated the cyt

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Ma, Sijia, Yang Qiu, and Chun Zhang. "Cytoskeleton Rearrangement in Podocytopathies: An Update." International Journal of Molecular Sciences 25, no. 1 (2024): 647. http://dx.doi.org/10.3390/ijms25010647.

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Podocyte injury can disrupt the glomerular filtration barrier (GFB), leading to podocytopathies that emphasize podocytes as the glomerulus’s key organizer. The coordinated cytoskeleton is essential for supporting the elegant structure and complete functions of podocytes. Therefore, cytoskeleton rearrangement is closely related to the pathogenesis of podocytopathies. In podocytopathies, the rearrangement of the cytoskeleton refers to significant alterations in a string of slit diaphragm (SD) and focal adhesion proteins such as the signaling node nephrin, calcium influx via transient receptor po

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Italiano, Joseph E., Murray Stewart, and Thomas M. Roberts. "Localized Depolymerization of the Major Sperm Protein Cytoskeleton Correlates with the Forward Movement of the Cell Body in the Amoeboid Movement of Nematode Sperm." Journal of Cell Biology 146, no. 5 (1999): 1087–96. http://dx.doi.org/10.1083/jcb.146.5.1087.

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The major sperm protein (MSP)-based amoeboid motility of Ascaris suum sperm requires coordinated lamellipodial protrusion and cell body retraction. In these cells, protrusion and retraction are tightly coupled to the assembly and disassembly of the cytoskeleton at opposite ends of the lamellipodium. Although polymerization along the leading edge appears to drive protrusion, the behavior of sperm tethered to the substrate showed that an additional force is required to pull the cell body forward. To examine the mechanism of cell body movement, we used pH to uncouple cytoskeletal polymerization a

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Hartwig, J. H., L. S. Jugloff, N. J. De Groot, S. A. Grupp, and J. Jongstra-Bilen. "The ligand-induced membrane IgM association with the cytoskeletal matrix of B cells is not mediated through the Ig alpha beta heterodimer." Journal of Immunology 155, no. 8 (1995): 3769–79. http://dx.doi.org/10.4049/jimmunol.155.8.3769.

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Abstract The B cell Ag receptor complex consists of membrane-associated Ig (mIg), Ig alpha, and Ig beta, associated molecules that have been implicated in transducing the activation signal that occurs upon receptor cross-linking. The role of the Ig alpha beta heterodimer in mediating binding to the cytoskeleton is unknown. We studied the ligand-induced association of mIgM with the cytoskeleton following receptor cross-linking in mIgM-expressing B lymphoma lines by biochemical assays, FACS analysis, and electron microscopy. Cytoskeletal association is not detected in unstimulated cells, but occ

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Chu, Cenfeng, Guisheng Zhong, and Hui Li. "Structure and function of subcortical periodic cytoskeleton throughout the nervous system." STEMedicine 1, no. 1 (2020): e9. http://dx.doi.org/10.37175/stemedicine.v1i1.9.

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Cytoskeleton plays an essential role in many functions in different cells and has been involved in the pathogenesis of many neural diseases. With the development of super-resolution fluorescence imaging technologies, which combine the molecular specificity and simple sample preparation of fluorescence microscopy and provide a spatial resolution comparable to that of electron microscopy, numerous new features have been revealed in the cytoskeletal organization of the subcortical cytoskeleton. A novel periodic lattice cytoskeleton is prevalent in different cell types throughout the nervous syste

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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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Haglund, Cat M., and Matthew D. Welch. "Pathogens and polymers: Microbe–host interactions illuminate the cytoskeleton." Journal of Cell Biology 195, no. 1 (2011): 7–17. http://dx.doi.org/10.1083/jcb.201103148.

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Intracellular pathogens subvert the host cell cytoskeleton to promote their own survival, replication, and dissemination. Study of these microbes has led to many discoveries about host cell biology, including the identification of cytoskeletal proteins, regulatory pathways, and mechanisms of cytoskeletal function. Actin is a common target of bacterial pathogens, but recent work also highlights the use of microtubules, cytoskeletal motors, intermediate filaments, and septins. The study of pathogen interactions with the cytoskeleton has illuminated key cellular processes such as phagocytosis, ma

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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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