Journal ArticleDOI
Two distinct actin networks drive the protrusion of migrating cells
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TLDR
Computational analysis of fluorescent speckle microscopy movies of migrating epithelial cells revealed this process is mediated by two spatially colocalized but kinematically, kinetically, molecularly, and functionally distinct actin networks.Abstract:
Cell migration initiates by extension of the actin cytoskeleton at the leading edge. Computational analysis of fluorescent speckle microscopy movies of migrating epithelial cells revealed this process is mediated by two spatially colocalized but kinematically, kinetically, molecularly, and functionally distinct actin networks. A lamellipodium network assembled at the leading edge but completely disassembled within 1 to 3 micrometers. It was weakly coupled to the rest of the cytoskeleton and promoted the random protrusion and retraction of the leading edge. Productive cell advance was a function of the second colocalized network, the lamella, where actomyosin contraction was integrated with substrate adhesion.read more
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Prediction of traction forces of motile cells.
Clément Roux,Clément Roux,Alain Duperray,Alain Duperray,Valérie M. Laurent,Valérie M. Laurent,Richard Michel,Richard Michel,Valentina Peschetola,Valentina Peschetola,Claude Verdier,Claude Verdier,Jocelyn Etienne,Jocelyn Etienne +13 more
TL;DR: A rheological model of actomyosin linking tension, deformation and myosin activity is validated and the basic pattern of traction forces is robustly predicted by the model and fixed parameters as a function of current geometry only.
Journal ArticleDOI
CAP1 (Cyclase-Associated Protein 1) Exerts Distinct Functions in the Proliferation and Metastatic Potential of Breast Cancer Cells Mediated by ERK.
Haitao Zhang,Guo-Lei Zhou +1 more
TL;DR: Findings that CAP1 exerts cell type-dependent functions in the invasiveness of breast cancer cells are reported and pivotal roles for the ERK-centered signaling in mediating both CAP1 functions are identified.
Journal ArticleDOI
p90 ribosomal S6 kinase (RSK) phosphorylates myosin phosphatase and thereby controls edge dynamics during cell migration.
Shiela C. Samson,Andrew Elliott,Brian D. Mueller,Yung Kim,Keith R. Carney,Jared P. Bergman,John Blenis,Michelle C. Mendoza,Michelle C. Mendoza +8 more
TL;DR: It is found that by inhibiting the myosin phosphatase, ERK and RSK promote myos in II–mediated tension for lamella expansion and optimal edge dynamics for cell migration, suggesting that ERK activity can coordinately amplify both protrusive and contractile forces for optimal cell motility.
Journal ArticleDOI
A three-component mechanism for fibroblast migration with a contractile cell body that couples a myosin II–independent propulsive anterior to a myosin II–dependent resistive tail
Wei-hui Guo,Yu-li Wang +1 more
TL;DR: Frontal, cell body, and rear regions perform distinct functions in the complex process of cell migration and a low-capacity, directional mechanism in the front coupled to a high- capacity, nondirectional mechanisms in the middle represents a highly appealing model for driving cell migration under high mechanical load.
Journal ArticleDOI
An update of knowledge on cortactin as a metastatic driver and potential therapeutic target in oral squamous cell carcinoma.
Pablo Ramos-García,Miguel Ángel González-Moles,Lucía González-Ruiz,Ángela Ayén,Isabel Ruiz-Ávila,Francisco J. Navarro‐Triviño,José Antonio Gil-Montoya +6 more
TL;DR: The prognostic implications of the oncogenic activation of cortactin in potentially malignant disorders and in head and neck cancer, where it appears to be relevant in the development of lymph node metastasis are analyzed.
References
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Journal ArticleDOI
Cell Migration: A Physically Integrated Molecular Process
TL;DR: The authors are grateful for financial support from the National Institutes of Health (grants GM23244 and GM53905), and to very helpful comments on the manuscript from Elliot Elson, Vlodya Gelfand, Paul Matsudaira, Julie Theriot, and Sally Zigmond.
Journal ArticleDOI
Cellular Motility Driven by Assembly and Disassembly of Actin Filaments
Thomas D. Pollard,Gary G. Borisy +1 more
TL;DR: A core set of proteins including actin, Arp2/3 complex, profilin, capping protein, and ADF/cofilin can reconstitute the process in vitro, and mathematical models of the constituent reactions predict the rate of motion.
Journal ArticleDOI
The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
TL;DR: It is shown that Arp2/3 complex purified from Acanthamoeba caps the pointed ends of actin filaments with high affinity and increases the critical concentration for polymerization at the pointed end from 0.6 to 1.0 microM.
Journal ArticleDOI
Dissecting Temporal and Spatial Control of Cytokinesis with a Myosin II Inhibitor
Aaron F. Straight,Amy Cheung,John Limouze,Irene A. Chen,Nicholas J. Westwood,James R. Sellers,Timothy J. Mitchison +6 more
TL;DR: It is shown that exit from the cytokinetic phase of the cell cycle depends on ubiquitin-mediated proteolysis and continuous signals from microtubules are required to maintain the position of the cleavage furrow, and these signals control the localization of myosin II independently of other furrow components.
Journal ArticleDOI
Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone.
Paul Forscher,Stephen J. Smith +1 more
TL;DR: Results suggest that actin normally polymerizes at the leading edge and then flows rearward at a rate between 3-6 microns/min, which is consistent with their being secondary to effects of CB on lamellar F-actin.
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