Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Academic Article uri icon

Overview

abstract

  • The multivesicular body (MVB) pathway is responsible for both the biosynthetic delivery of lysosomal hydrolases and the downregulation of numerous activated cell surface receptors which are degraded in the lysosome. We demonstrate that ubiquitination serves as a signal for sorting into the MVB pathway. In addition, we characterize a 350 kDa complex, ESCRT-I (composed of Vps23, Vps28, and Vps37), that recognizes ubiquitinated MVB cargo and whose function is required for sorting into MVB vesicles. This recognition event depends on a conserved UBC-like domain in Vps23. We propose that ESCRT-I represents a conserved component of the endosomal sorting machinery that functions in both yeast and mammalian cells to couple ubiquitin modification to protein sorting and receptor downregulation in the MVB pathway.

publication date

  • July 27, 2001

Research

keywords

  • Carrier Proteins
  • Endosomes
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitins
  • Vesicular Transport Proteins

Identity

Scopus Document Identifier

  • 0035958546

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(01)00434-2

PubMed ID

  • 11511343

Additional Document Info

volume

  • 106

issue

  • 2