期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 103, 期 16, 页码 6202-6207出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0601712103
关键词
endosome; ESCRT complexes; protein sorting; Vps; class E
资金
- NICHD NIH HHS [T32 HD007348, HD07348] Funding Source: Medline
- NIGMS NIH HHS [GM07759, R01 GM032448, R37 GM032448, GM32448, T32 GM007759] Funding Source: Medline
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.
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