The regulation of integrin function by Ca2+

被引：124

作者：

Leitinger, B ^{[1
]}

McDowall, A ^{[1
]}

Stanley, P ^{[1
]}

Hogg, N ^{[1
]}

机构：

[1] Imperial Canc Res Fund, Leukocyte Adhes Lab, London WC2A 3PX, England

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2000年 / 1498卷 / 2-3期

关键词：

Ca2+; divalent cation; integrin; inserted domain; adhesion;

D O I：

10.1016/S0167-4889(00)00086-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Integrins are metalloproteins whose receptor function is dependent on the interplay between Mg2+ and Ca2+. Although the specificity of the putative divalent cation binding sites has been poorly understood, some issues are becoming clearer and this review will focus on the more recent information. The MIDAS motif is a unique Mg2+/Mn2+ binding site located in the integrin alpha subunit I domain. Divalent cation bound at this site has a structural role in coordinating the binding of ligand to the I domain containing integrins. The I-like domain of the integrin beta subunit also has a MIDAS-like motif but much less is known about its cation binding preferences. The N-terminal region of the integrin a subunit has been modelled as a beta -propeller, containing three or four 'EF hand' type divalent cation binding motifs for which the function is ill defined. It seems certain that most integrins have a high affinity Ca2+ site which is critical for alpha beta heterodimer formation, but the location of this site is unknown. Finally intracellular Ca2+ fluxes activate the Ca2+ requiring enzyme, calpain, which regulates cluster formation of leucocyte integrins. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：91 / 98

页数：8

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