The cytoplasmic domain of the α1 integrin subunit influences stress fiber formation via the conserved GFFKR motif

被引:18
作者
Vossmeyer, D [1 ]
Kaufmann, C [1 ]
Löster, K [1 ]
Lucka, L [1 ]
Horstkorte, R [1 ]
Reutter, W [1 ]
Danker, K [1 ]
机构
[1] Free Univ Berlin, Inst Mol Biol & Biochem, D-14195 Berlin, Germany
关键词
alpha; 1; beta; 1-integrin; cytoplasmic deletion; actin cytoskeleton; stress fiber formation; migration;
D O I
10.1006/excr.2000.4831
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Integrins are heterodimeric transmembrane proteins that mediate substrate adhesion and migration but also the bidirectional transfer of information across the plasma membrane via their cytoplasmic domains. me addressed the question of whether the very short cytoplasmic tail of the alpha 1 integrin subunit of alpha 1 beta 1 integrin is required for alpha 1 beta 1-specific adhesion, spreading, and migration. For this purpose we transfected the alpha 1 integrin subunit and two cytoplasmically truncated alpha 1 subunits into Chinese hamster ovary (CHO) cells. Elimination of the entire cytoplasmic domain of the alpha 1 subunit does not affect adhesion but leads to inhibition of spreading and stress fiber formation. The defect in spreading could not be rescued by lysophosphatidic acid, which has been reported to stimulate actin stress fiber formation via Rho. Additionally, deletion of the entire cytoplasmic domain of the alpha 1 subunit abolishes migration toward alpha 1 beta 1-specific substrates. Migration and stress fiber formation are similar in CHO-alpha 1 cells and CHO cells carrying an alpha 1 subunit still containing the conserved GFFKR motif. So, the GFFKR motif of the al subunit is essential and sufficient for these processes. (C) 2000 Academic Press.
引用
收藏
页码:321 / 327
页数:7
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