Structural and functional analysis of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m
Structural and functional analysis of the putative inositol 1,3,4,5-tetrakisphosphate receptors GAP1IP4BP and GAP1m
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DOI：
10.1006/bbrc.1998.9179
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发表时间：
1998-09-08
影响因子：
3.1
通讯作者：
Cullen, PJ
中科院分区：
文献类型：
--
作者：
Bottomley, JR;Reynolds, JS;Cullen, PJ
以前，我们已经纯化并克隆了一种高亲和力异构特异性肌醇1，3，4，5-四磷酸（Ins（1，3，4，5）P-4）结合蛋白，因为它显然是Ras GTP酶激活蛋白（GAP）的GAP 1家族的成员，我们将其称为GAP 1（IP 4 BP）。在这里，我们表明，表达的全长GAP 1（IP 4 BP）与Ins（1，3，4，5）P-4结合的亲和力和特异性类似于最初纯化的蛋白质，结合活性依赖于功能性PH/Btk结构域。此外，我们强调了GAP 1（IP 4 BP）及其同源物GAP 1（m）之间的根本区别，即两种蛋白质都具有Ras GAP的功能，但只有GAP 1（IP 4 BP）显示Rap GAP活性。(C)北京：科学出版社.
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.