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Eur J Cell Biol. 2006 Apr;85(3-4):275-82. Epub 2005 Nov 16.

Unraveling ICAP-1 function: toward a new direction?

Author information

1
LEDAC, UMR CNRS/UJF 5538, Institut Albert Bonniot, Domaine de la Merci, Faculté de Médecine, F-38706 La Tronche Cedex, France. daniel.bouvard@ujf-grenoble.fr

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.

PMID:
16546571
DOI:
10.1016/j.ejcb.2005.10.005
[Indexed for MEDLINE]

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