Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Academic Article uri icon

Overview

abstract

  • The sequential action of the Vps27/HRS complex, ESCRT-I, -II, and -III is required to sort ubiquitinated transmembrane proteins to the lumen of lysosomes via the multivesicular body (MVB) pathway. While Vps27/HRS, ESCRT-I, and -II are recruited to endosomes as preformed complexes, the ESCRT-III subunits Vps20, Snf7, Vps24, and Vps2 only assemble into a complex on endosomes. We have addressed the pathway and the regulation for ESCRT-III assembly. Our findings indicate the ordered assembly of a transient 450 kDa ESCRT-III complex on endosomes. Despite biochemical and structural similarity, each subunit contributes a specific function. Vps20 nucleates transient oligomerization of Snf7, which appears to sequester MVB cargo. Vps24 terminates Snf7 oligomerization by recruiting Vps2, which subsequently engages the AAA-ATPase Vps4 to dissociate ESCRT-III. We propose that the ordered assembly and disassembly of ESCRT-III delineates an MVB sorting domain to sequester cargo and complete the last steps of MVB sorting.

publication date

  • October 1, 2008

Research

keywords

  • Endosomes
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins
  • Transport Vesicles
  • Vesicular Transport Proteins

Identity

Scopus Document Identifier

  • 53249131094

Digital Object Identifier (DOI)

  • 10.1016/j.devcel.2008.08.013

PubMed ID

  • 18854142

Additional Document Info

volume

  • 15

issue

  • 4