Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body

被引：76

作者：

Lottridge, JM ^{[1
]}

Flannery, AR ^{[1
]}

Vincelli, JL ^{[1
]}

Stevens, TH ^{[1
]}

机构：

[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2006年 / 103卷 / 16期

关键词：

endosome; ESCRT complexes; protein sorting; Vps; class E;

D O I：

10.1073/pnas.0601712103

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：

Previous two-hybrid analysis of the 17 soluble class E Vps yeast proteins revealed that Vps46p/Did2p interacts with Vta1p and the AAA (ATPase associated with a variety of cellular activities) ATPase Vps4p. Here we report that the binding of Vps46p to Vps4p and Vta1p is direct and not mediated by additional proteins, and the binding of Vps46p to Vps4p is ATP independent. Vps46p regulates the membrane association of Vps4p and is required for the interaction of Vta1p with Vps32p/Snf7p of the ESCRT-III complex. Vta1p is a potent activator of Vps4p, stimulating the ATPase activity by 6- to 8-fold. These results reveal functional roles for the Vps46p and Vta1p proteins in regulating the ESCRT complex assembly/disassembly cycle in protein sorting at the yeast late endosome.

引用

页码：6202 / 6207

页数：6

共 32 条

[1] The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function [J].