Biogenesis and function of multivesicular bodies

Robert C. Piper, David J. Katzmann

Research output: Contribution to journalReview article

407 Scopus citations

Abstract

The two major cellular sites for membrane protein degradation are the proteasome and the lysosome. Ubiquitin attachment is a sorting signal for both degradation routes. For lysosomal degradation, ubiquitination triggers the sorting of cargo proteins into the lumen of late endosomal multivesicular bodies (MVBs)/endosomes. MVB formation occurs when a portion of the limiting membrane of an endosome invaginates and buds into its own lumen. Intralumenal vesicles are degraded when MVBs fuse to lysosomes. The proper delivery of proteins to the MVB interior relies on specific ubiquitination of cargo, recognition and sorting of ubiquitinated cargo to endosomal subdomains, and the formation and scission of cargo-filled intralumenal vesicles. Over the past five years, a number of proteins that may directly participate in these aspects of MVB function and biogenesis have been identified. However, major questions remain as to exactly what these proteins do at the molecular level and how they may accomplish these tasks.

Original languageEnglish (US)
Pages (from-to)519-547
Number of pages29
JournalAnnual Review of Cell and Developmental Biology
Volume23
DOIs
StatePublished - Dec 1 2007

Keywords

  • Downregulation
  • ESCRT
  • Endosome
  • Lysosome
  • Peptidase
  • Ubiquitin

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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