Editors' ChoiceReview

"Cas"ting New Light on Integrin Signaling

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Science's STKE  07 Mar 2000:
Vol. 2000, Issue 22, pp. tw1
DOI: 10.1126/stke.2000.22.tw1

Cell morphology is regulated by anchorage to extracellular matrices and is determined intracellularly by actin scaffolds and focal adhesion formation. In response to the changes in the extracellular matrix, signaling networks aggregate on actin filaments and direct changes in adhesion and cell shape. Recent advances in understanding integrin signaling have revealed the important regulatory role for the Crk-associated substrate (Cas) family of docking proteins. The Cas family comprises p130Cas, HEF1/Cas-L, and Efs/Sin; all function as key bridging proteins in actin-associated signaling. p130Cas was first identified as a phosphotyrosyl substrate of an oncogenic Src mutant, but it is unclear whether Cas proteins are essential for the transformed cellular phenotype. O'Neill et al. review the role of Cas proteins in integrin signaling. The authors discuss the function of the separate domains within Cas family proteins; the proteins that associate with Cas; and the functional roles for Cas proteins in different cellular processes. Whether functional redundancy exists between the known Cas family members is not known; however, each protein's Src-homology 3 (SH3) domain displays differential binding affinities for various signaling proteins in vitro.

O'Neill, G.M., Fashena, S.J., and Golemis, E.A. (2000) Integrin signalling: a new Cas(t) of characters enters the stage. Trends Cell Biol. 10: 111-119 [Online Journal]

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