Bidirectional signaling between the cytoskeleton and integrins

Current Opinion in Cell Biology

Volumn 11, Issue 2, 1999, Pages 274-286

  Schoenwaelder, Simone M ^a   Burridge, Keith ^a,b  

^a Dept of Environ Sci and Eng   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE; CYTOSKELETON PROTEIN; GUANOSINE TRIPHOSPHATASE; INTEGRIN; MYOSIN; PROTEIN TYROSINE KINASE; RHO FACTOR; SCLEROPROTEIN;

CELL ADHESION; CELL MOTILITY; CYTOSKELETON; DEPHOSPHORYLATION; INTERMEDIATE FILAMENT; LAMELLIPODIUM; MICROTUBULE; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION;

EID: 0032911020     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80037-4     Document Type: Article

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125. Kaverina I., Rottner K., Small J.V. Targeting, capture, and stabilization of microtubules at early focal adhesions. J Cell Biol. 142:1998;181-190. The authors present evidence that microtubules target focal adhesions and that their capture by focal adhesions stabilizes them against depolymerization. They suggest that the effect of RhoA enhancing microtubule stability may be due to RhoA stimulating focal adhesion assembly.
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130. Clark E.A., King W.G., Brugge J.S., Symons M., Hynes R.O. Integrin-mediated signals regulated by members of the Rho family of GTPases. J Cell Biol. 142:1998;573-586. Integrin-ligation results in the activation of Rho family GTPases. In the absence of growth factors, membrane ruffling during integrin-mediated adhesion and spreading is dependent on Cdc42 and Rac. Rho controls the clustering and formation of larger focal adhesions and Rho regulates the majority of FAK and paxillin phosphorylation. Cdc42 regulates Akt and Erk2 activation.
131. Price L.S., Leng J., Schwartz M.A., Bokoch G.M. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol Biol Cell. 9:1998;1863-1871. Integrin-mediated adhesion is shown to activate Cdc42 and Rac. These GTPases are critical for cell sprading.
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133. Polte T.R., Hanks S.K. Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc Natl Acad Sci USA. 92:1995;10678-10682.
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136. Nojima Y., Morino N., Mimura T., Hamasaki K., Furuya H., Sakai R., Sato T., Tachibana K., Morimoto C., Yazaki Y., Hirai H. Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homolgy 2-binding motifs. J Biol Chem. 270:1995;15398-15402.
137. Vuori K., Ruoslahti E. Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix. J Biol Chem. 270:1995;22259-22262.
138. cas to the guanine nucleotide exchange factor C3G. J Biol Chem. 273:1998;25673-25679.
139. Cas. Nat Genet. 19:1998;361-365. Fibroblasts from mice with the gene for Cas disrupted show defective formation of stress fibers and focal adhesions, suggesting that Rho activity may be affected.
140. •] in the context of Rho activation via Cas and Crk.
141. Altun-Gultekin Z.F., Chandriani S., Bougeret C., Ishizaki T., Narumiya S., Degraaf P., Henegouwen P.V.E., Hanafusa H., Wagner J.A., Birge R.B. Activation of Rho-dependent cell spreading and focal adhesion biogenesis by the v-crk adaptor protein. Mol Cell Biol. 18:1998;3044-3058. The authors provide evidence suggesting that expression of the adapter protein v-crk in PC12 cells activates the Rho signaling pathway.
142. cas as a mediator of focal adhesion kinase-promoted cell migration. J Cell Biol. 140:1998;211-221. The authors demonstrate that Cas, acting as part of a FAK/Cas complex, plays an important role in FAK-mediated cell migration. Co-expression of Cas in CHO cells overexpressing FAK increased cell migration above the level induced by FAK overexpression alone. Co-expression of the SH3 domain of Cas (acting as a dominant-negative) decreased cell migration.
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