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
Citations
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Journal ArticleDOI
Focal adhesion and actin organization by a cross-talk of TM4SF5 with integrin α2 are regulated by serum treatment
TL;DR: The functions of TM4 SF5 collaborative with integrin signaling to alter focal contact dynamics, actin reorganization, and migration are revealed and a mechanism of cross-talk between TM4SF5 and integrin which is further regulated by growth factor signaling is suggested.
Journal ArticleDOI
Psidin, a conserved protein that regulates protrusion dynamics and cell migration
Ji Hoon Kim,Aeri Cho,Hongyan Yin,Dorothy A. Schafer,Ghassan Mouneimne,Kaylene J. Simpson,Kim Vy Nguyen,Joan S. Brugge,Denise J. Montell +8 more
TL;DR: Psid is an actin regulatory protein that plays a conserved role in protrusion dynamics and cell migration and is screened for new genes that regulate cell movement in vivo.
Journal ArticleDOI
Communicating Subcellular Distributions
TL;DR: This review describes current progress towards determining and representing protein subcellular patterns so that the information can be used as part of systems biology efforts.
Journal ArticleDOI
Profiling cellular morphodynamics by spatiotemporal spectrum decomposition.
TL;DR: A framework to profile cellular morphodynamics based on an adaptive decomposition of local cell boundary motion into instantaneous frequency spectra defined by the Hilbert-Huang transform is implemented and finds that subcellular regions with different morphodynamics indeed exhibit distinct Rac1 activities.
Journal ArticleDOI
Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation.
Prabuddha Gupta,Nils C. Gauthier,Yu Cheng-Han,Yuan Zuanning,Bruno Pontes,Malte Ohmstede,Malte Ohmstede,René Martin,Hans-Joachim Knölker,Hans-Günther Döbereiner,Hans-Günther Döbereiner,Mira Krendel,Michael P. Sheetz +12 more
TL;DR: It is suggested that, by moving to actin polymerization sites and early adhesion sites in active lamellipodia, Myosin 1E might play important roles in transporting not only important polymerizing proteins but also proteins involved in adhesion stabilization.
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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