Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains

被引：357

作者：

Klarlund, JK ^{[1
]}

Guilherme, A ^{[1
]}

Holik, JJ ^{[1
]}

Virbasius, JV ^{[1
]}

Chawla, A ^{[1
]}

Czech, MP ^{[1
]}

机构：

[1] UNIV MASSACHUSETTS, MED CTR, DEPT BIOCHEM & MOL BIOL, WORCESTER, MA 01605 USA

来源：

SCIENCE | 1997年 / 275卷 / 5308期

关键词：

D O I：

10.1126/science.275.5308.1927

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3' position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1 was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P-3] through a pleckstrin homology (PH) domain and displaysa region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin beta 2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P-3. GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.

引用

页码：1927 / 1930

页数：4

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