Structural and functional analysis of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m

被引：25

作者：

Bottomley, JR ^{[1
]}

Reynolds, JS ^{[1
]}

Lockyer, PJ ^{[1
]}

Cullen, PJ ^{[1
]}

机构：

[1] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 250卷 / 01期

基金：

英国生物技术与生命科学研究理事会; 英国医学研究理事会;

关键词：

Ras; Rap; GAPs; Ins(1,3,4,5)P-4; GAP1(IP4BP); GAP1(m);

D O I：

10.1006/bbrc.1998.9179

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：

Previously we have purified and cloned a high affinity isomerically specific inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P-4)-binding protein which, because it is clearly a member of the GAP1 family of Ras GTPase-activating proteins (GAP), we have termed GAP1(IP4BP). Here we show that expressed full-length GAP1(IP4BP) binds Ins(1,3,4,5)P-4 with an affinity and specificity similar to that of the originally purified protein, a binding activity which is dependent on a functional PH/Btk domain. Furthermore, we highlight a fundamental distinction between GAP1(IP4BP) and its homologue GAP1(m), namely that both proteins function as Ras GAPs but only GAP1(IP4BP) displays Rap GAP activity. (C) 1998 Academic Press.

引用

页码：143 / 149

页数：7

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