Talin and vinculin play distinct roles in filopodial motility in the neuronal growth cone.

Sydor, A M; Su, A L; Wang, F S; Xu, A; Jay, Daniel G.

doi:10.1083/jcb.134.5.1197

Cited by 107 publications

(113 citation statements)

References 43 publications

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“…These observations resemble the finding that disruption of myosin IIA reduced cell adhesion of mouse neuroblastoma cells (Wylie and Chantler, 2001). Furthermore, CALI of vinculin, a component of focal contacts, in growth cones also caused filopodia to detach and buckle (Sydor et al, 1996). Thus, myosin II inhibition with blebbistatin may disrupt adhesion of filopodia, and we speculate the increased filopodial extension rates are attributable to reduced membrane cortical tension and altered actin dynamics (Mallavarapu and Mitchison, 1999;Raucher and Sheetz, 2000).…”

Section: -D ( S)-(ϫ)-supporting

confidence: 63%

Brain-Derived Neurotrophic Factor Regulation of Retinal Growth Cone Filopodial Dynamics Is Mediated through Actin Depolymerizing Factor/Cofilin

Gehler¹,

Shaw²,

Sarmiere³

et al. 2004

J. Neurosci.

112

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The molecular mechanisms by which neurotrophins regulate growth cone motility are not well understood. This study investigated the signaling involved in transducing BDNF-induced increases of filopodial dynamics. Our results indicate that BDNF regulates filopodial length and number through a Rho kinase-dependent mechanism. Additionally, actin depolymerizing factor (ADF)/cofilin activity is necessary and sufficient to transduce the effects of BDNF. Our data indicate that activation of ADF/cofilin mimics the effects of BDNF on filopodial dynamics, whereas ADF/cofilin inactivity blocks the effects of BDNF. Furthermore, BDNF promotes the activation of ADF/ cofilin by reducing the phosphorylation of ADF/cofilin. Although inhibition of myosin II also enhances filopodial length, our results indicate that BDNF signaling is independent of myosin II activity and that the two pathways result in additive effects on filopodial length. Thus, filopodial extension is regulated by at least two independent mechanisms. The BDNF-dependent pathway works via regulation of ADF/cofilin, independently of myosin II activity.

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Section: -D ( S)-(ϫ)-supporting

confidence: 63%

Brain-Derived Neurotrophic Factor Regulation of Retinal Growth Cone Filopodial Dynamics Is Mediated through Actin Depolymerizing Factor/Cofilin

Gehler¹,

Shaw²,

Sarmiere³

et al. 2004

J. Neurosci.

112

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“…Associated with focal adhesions and focal complexes are numerous signaling proteins including FAK, and structural proteins including paxillin and vinculin (41,45,46). When cells adhered to fibronectin or laminin, paxillin and talin are found in typical focal adhesion structures distributed over the cell bodies, as previously reported (30,44,47) (Fig.…”

Section: Fibroblast Adhesion To Cyr61 or Ctgf Induces Extensive And Psupporting

confidence: 57%

The Angiogenic Factors Cyr61 and Connective Tissue Growth Factor Induce Adhesive Signaling in Primary Human Skin Fibroblasts

Chen

Lau

2001

Journal of Biological Chemistry

289

279

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The angiogenic inducers cysteine-rich angiogenic protein 61 (Cyr61) and connective tissue growth factor (CTGF) are structurally related, extracellular matrixassociated heparin-binding proteins. Both can stimulate chemotaxis and promote proliferation in endothelial cells and fibroblasts in culture and induce neovascularization in vivo. Encoded by inducible immediate early genes, Cyr61 and CTGF are synthesized upon growth factor stimulation in cultured fibroblasts and during cutaneous wound healing in dermal fibroblasts. Recently, we have shown that adhesion of primary human fibroblasts to immobilized Cyr61 is mediated through integrin ␣ 6 ␤ 1 and cell surface heparan sulfate proteoglycans (HSPGs) (Chen, N., Chen, C.-C., and Lau, L.F. (2000) J. Biol. Chem. 275, 24953-24961), providing the first demonstration of an absolute requirement for HSPGs in integrin-mediated cell attachment. We show in this study that CTGF also mediates fibroblast adhesion through the same mechanism and demonstrate that fibroblasts adhesion to immobilized Cyr61 or CTGF induces distinct adhesive signaling responses consistent with their biological activities. Compared with fibroblast adhesion to fibronectin, laminin, or type I collagen, cell adhesion to Cyr61 or CTGF induces 1) more extensive and prolonged formation of filopodia and lamellipodia, concomitant with formation of integrin ␣ 6 ␤ 1 -containing focal complexes localized at leading edges of pseudopods; 2) activation of intracellular signaling molecules including focal adhesion kinase, paxillin, and Rac with similar rapid kinetics; 3) sustained activation of p42/p44 MAPKs lasting for at least 9 h; and 4) prolonged gene expression changes including up-regulation of MMP-1 (collagenase-1) and MMP-3 (stromelysin-1) mRNAs and proteins sustained for at least 24 h. Together, these results establish Cyr61 and CTGF as bona fide adhesive substrates with specific signaling capabilities, provide a molecular basis for their activities in fibroblasts through integrin ␣ 6 ␤ 1 and HSPG-mediated signaling during attachment and indicate that these proteins may function in matrix remodeling through the activation of metalloproteinases during angiogenesis and wound healing.

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“…In situ experiments using chromophore-assisted laser inactivation (CALI) have implicated talin as a crucial molecule in the ECMactin linkage during filopodial extension and retraction (Sydor et al, 1996). More recently, extensive characterization of actin dynamics using fluorescent speckle microscopy (FSM) (Waterman-Storer et al, 1998) has revealed two spatially, kinetically and kinematically distinct actin networks; with the local expansion of the lamella network being a source of persistent cell protrusion (Ponti et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Probing the integrin-actin linkage using high-resolution protein velocity mapping

Brown

Hébert

Kolin

et al. 2006

Journal of Cell Science

162

166

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Cell migration is regulated in part by the connection between the substratum and the actin cytoskeleton. However, the very large number of proteins involved in this linkage and their complex network of interactions make it difficult to assess their role in cell migration. We apply a novel image analysis tool, spatio-temporal image correlation spectroscopy (STICS), to quantify the directed movements of adhesion-related proteins and actin in protrusions of migrating cells. The STICS technique reveals protein dynamics even when protein densities are very low or very high, and works in the presence of large, static molecular complexes. Detailed protein velocity maps for actin and the adhesion-related proteins α-actinin, α5-integrin, talin, paxillin, vinculin and focal adhesion kinase are presented. The data show that there are differences in the efficiency of the linkage between integrin and actin among different cell types and on the same cell type grown on different substrate densities. We identify potential mechanisms that regulate efficiency of the linkage, or clutch, and identify two likely points of disconnect, one at the integrin and the other at α-actinin or actin. The data suggests that the efficiency of the linkage increases as actin and adhesions become more organized showing the importance of factors that regulate the efficiency in adhesion signaling and dynamics.

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Talin and vinculin play distinct roles in filopodial motility in the neuronal growth cone.

Cited by 107 publications

References 43 publications

Brain-Derived Neurotrophic Factor Regulation of Retinal Growth Cone Filopodial Dynamics Is Mediated through Actin Depolymerizing Factor/Cofilin

Brain-Derived Neurotrophic Factor Regulation of Retinal Growth Cone Filopodial Dynamics Is Mediated through Actin Depolymerizing Factor/Cofilin

The Angiogenic Factors Cyr61 and Connective Tissue Growth Factor Induce Adhesive Signaling in Primary Human Skin Fibroblasts

Probing the integrin-actin linkage using high-resolution protein velocity mapping

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