Mapping the site of interaction between annexin VI and the p120GAP C2 domain

被引：16

作者：

Chow, A ^{[1
]}

Gawler, D ^{[1
]}

机构：

[1] Univ Leeds, Sch Biomed Sci, Leeds LS2 9JT, W Yorkshire, England

来源：

FEBS LETTERS | 1999年 / 460卷 / 01期

关键词：

conserved region 2; GTPase activating protein; Ras; annexin; Ca2+;

D O I：

10.1016/S0014-5793(99)01336-8

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：

Annexin VI is a Ca2+-dependent membrane and phospholipid binding protein. It mediates a protein-protein interaction with the Pas p21 regulatory protein p120(GAP). In this study me have mapped the binding site of GAP within the annexin VI protein. Using Far Western overlay binding assays and cell lysate competition studies we have mapped the site of interaction to the inter-lobe linker region; amino acids 325-363, Finally, using a GST fusion protein corresponding to this linker region me have demonstrated that cellular loading of the fusion protein into Rat-1 fibroblasts by electroporation blocks the interaction and co-immunoprecipitation of annexin VI and GAP. (C) 1999 Federation of European Biochemical Societies.

引用

页码：166 / 172

页数：7

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