Cited by 771Cellular transport and secretionAutophagy in Disease and TherapyUbiquitin and proteasome pathways

Biogenesis and Function of Multivesicular Bodies

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Piper, Robert C., Katzmann, David J.·2007·Annual Review of Cell and Developmental Biology

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.

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Crossref · 10.1146/annurev.cellbio.23.090506.123319

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Authors
Piper, R. C., & Katzmann, D. J.
Affiliations
  • University of Iowa (US)
  • Mayo Clinic (US)
Venue
Annual Review of Cell and Developmental Biology
Published
2007-11-01
Volume
23
Issue
1
Pages
519-547
ISSN
  • 1081-0706 (ISSN-L)
  • 1530-8995
OpenAlex
W2109691647
Cited by
771
References
154
Citations by year
2026: 23 · 2025: 34 · 2024: 55 · 2023: 39 · 2022: 51 · 2021: 49 · 2020: 48 · 2019: 54 · 2018: 46 · 2017: 36 · 2016: 28 · 2015: 37 · 2014: 26 · 2013: 34 · 2012: 38
FWCI
3.06
Type
journal article
Language
en
Open access
Locations
  • Annual Review of Cell and Developmental Biology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (R01GM58202, R01GM73024, R01GM073024, R01GM058202)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
multivesicular bodies, endosomes, membrane protein degradation, ubiquitination, lysosomal degradation, proteasome, intralumenal vesicles, endosomal sorting, cargo sorting, membrane fission
MeSH terms
Animals, Humans, Lysosomes, Protein Conformation, Proteins, Endosomes, Protein Transport, Protein Sorting Signals, Ubiquitin, Lipid Metabolism, Ubiquitination

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