Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24

被引：109

作者：

Ghazi-Tabatabai, Sara ^{[1
]}

Saksena, Suraj ^{[2
]}

Short, Judith M. ^{[1
]}

Pobbati, Ajaybabu V. ^{[1
]}

Veprintsev, Dmitry B. ^{[1
]}

Crowther, R. Anthony ^{[1
]}

Emr, Scott D. ^{[2
]}

Egelman, Edward H. ^{[3
]}

Williams, Roger L. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Cornell Univ, Cornell Inst Cell & Mol Biol, Dept Mol Biol & Genet, Ithaca, NY 14853 USA

[3] Univ Virginia, Hlth Sci Ctr, Dept Biochem & Mol Genet, Charlottesville, VA 22908 USA

来源：

STRUCTURE | 2008年 / 16卷 / 09期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/j.str.2008.06.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ESCRT machinery mediates sorting of ubiquitinated transmembrane proteins to lysosomes via multivesicular bodies (MVBs) and also has roles in cytokinesis and viral budding. The ESCRT-III subunits are metastable monomers that transiently assemble on membranes. However, the nature of these assemblies is unknown. Among the core yeast ESCRT-III subunits, Snf7 and Vps24 spontaneously form ordered polymers in vitro. Single-particle EM reconstruction of helical Vps24 filaments shows both parallel and head-to-head subunit arrangements. Mutations of regions involved in intermolecular assembly in vitro result in cargo-sorting defects in vivo, suggesting that these homopolymers mimic interactions formed by ESCRT-III heteropolymers during MVB biogenesis. The C terminus of Vps24 is at the surface of the filaments and is not required for filament assembly. When this region is replaced by the MIT-interacting motif from the Vps2 subunit of ESCRT-III, the AAA-ATPase Vps4 can both bundle and disassemble the chimeric filaments in a nucleotide-dependent fashion.

引用

页码：1345 / 1356

页数：12

共 58 条

[1] Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo [J].