Role of two conserved glycine residues in the β-propeller domain of the integrin α4 subunit in VLA-4 conformation and function

被引：8

作者：

Guerrero-Esteo, M ^{[1
]}

Ruiz-Velasco, N ^{[1
]}

Muñoz, M ^{[1
]}

Teixidó, J ^{[1
]}

机构：

[1] Ctr Invest Biol, E-28006 Madrid, Spain

来源：

FEBS LETTERS | 1998年 / 429卷 / 01期

关键词：

alpha; 4; integrin; beta-propeller; adhesion;

D O I：

10.1016/S0014-5793(98)00576-6

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：

The N-terminal region of the alpha integrin subunits is predicted to fold into a beta-propeller domain. Using K562 alpha 4 transfectants we show that mutations at alpha 4 subunit residues Gly(130) and Gly(190) affect the conformation of this domain causing a reduction in the recognition of alpha 4 by anti-alpha 4 antibodies which map to the beta-propeller, The improper alpha 4 conformation also led to an altered association with the beta 1 subunit, and to a lack of alpha 4 beta 1 adhesion to VCAM-1 and CS-1/fibronectin, as well as an abolishment of anti-alpha 4- and anti-beta 1-dependent homotypic aggregation. The total conservation of Gly(130) and Gly(190) among integrin alpha subunits suggests their importance in the correct folding of their respective beta-propeller domains, and thus, in the adhesive activity of the integrins, (C) 1998 Federation of European Biochemical Societies.

引用

页码：123 / 128

页数：6