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解析ICAP-1的功能:朝着新方向发展?

Unraveling ICAP-1 function: toward a new direction?

作者信息

Bouvard Daniel, Millon-Fremillon Angélique, Dupe-Manet Sandra, Block Marc R, Albiges-Rizo Corinne

机构信息

LEDAC, UMR CNRS/UJF 5538, Institut Albert Bonniot, Domaine de la Merci, Faculté de Médecine, F-38706 La Tronche Cedex, France.

出版信息

Eur J Cell Biol. 2006 Apr;85(3-4):275-82. doi: 10.1016/j.ejcb.2005.10.005. Epub 2005 Nov 16.

Abstract

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 non-covalently 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 beta1 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.

摘要

在生理和病理情况下,细胞与细胞外基质(ECM)或相邻细胞的黏附都至关重要。整合素是一大类细胞黏附受体,由两个非共价连接的α和β亚基组成。它们具有明确的双重功能,即介导牢固黏附和信号传导。整合素的短细胞质结构域可与几种不同整合素共享的细胞质蛋白或特定类型整合素特有的细胞质蛋白相互作用。整合素细胞质结构域相关蛋白-1(ICAP-1)是一种小的细胞质蛋白,它与β1整合素亚基特异性相互作用。在本综述中,我们将讨论关于ICAP-1的最新发现,不仅涉及结构和功能层面,还涉及其在其他信号通路(如控制细胞增殖的信号通路)中可能的相互联系。

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