A functional PtdIns(3)P-binding motif

被引：250

作者：

Patki, V ^{[1
]}

Lawe, DC

Corvera, S

Virbasius, JV

Chawla, A

机构：

[1] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA

[2] Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01605 USA

来源：

NATURE | 1998年 / 394卷 / 6692期

关键词：

D O I：

10.1038/28771

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：

Treating cells with the phosphatidylinositol-3-OH kinase (PI(3)K) inhibitor wortmannin causes the dissociation of the early-endosomal antigen EEA1 from early endosomes1. EEA1 from cytosolic extracts binds to liposomes containing phosphatidylinositol-3-phosphate (PtdIns(3)P), the major product of PI(3)K in yeast and mammalian cells1,2. Here we show that a RING zinc-finger domain at the carboxy terminus of EEA1, previously identified and named the ‘FYVE’ domain3, binds directly and specifically to PtdIns(3)P. This indicates that proteins containing this motif may be downstream effectors of PI(3)K in yeast and mammalian cells.

引用

页码：433 / 434

页数：2

共 11 条

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