Unraveling ICAP-1 function: Toward a new direction?

被引：18

作者：

Bouvard, D ^{[1
]}

Millon-Fremillon, A ^{[1
]}

Dupe-Manet, S ^{[1
]}

Block, MR ^{[1
]}

Albiges-Rizo, C ^{[1
]}

机构：

[1] Inst Albert Bonniot, CNRS, UMR UJF 5538, LEDAC,Fac Med, F-38706 La Tronche, France

来源：

EUROPEAN JOURNAL OF CELL BIOLOGY | 2006年 / 85卷 / 3-4期

关键词：

ICAP-1; integrin signaling; Krit-1; Nm23-H2;

D O I：

10.1016/j.ejcb.2005.10.005

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Cell adhesion to either the extracellular matrix (ECM) or to neighboring cells is of critical importance during both physiological and pathological situations. Integrins are a large family of cell adhesion receptors composed of two noncovalently linked alpha and beta subunits. They have a well-identified dual function of mediating both firm adhesion and signaling. The short cytoplasmic domain of integrin can interact with cytoplasmic proteins that are either shared by several different integrins or specific for one type of integrin. Integrin cytoplasmic domain-associated protein-1 (ICAP-1) is a small cytoplasmic protein that specifically interacts with the beta(1) integrin subunit. In this review we will discuss recent findings on ICAP-1, not only at the Structural and functional level, but also its possible interconnection in other signaling pathways such as those that control cell proliferation. (c) 2005 Elsevier GmbH. All rights reserved.

引用

页码：275 / 282

页数：8

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