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

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Biogenesis and Function of Multivesicular Bodies

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

DOI 10.1146/annurev.cellbio.23.090506.123319PMC PMC2911632

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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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Authors: Piper, R. C., & Katzmann, D. J.
Affiliations: University of Iowa (US)
Mayo Clinic (US)
ORCID: Piper, Robert C.
Katzmann, David J.
Venue: Annual Review of Cell and Developmental Biology
Publisher: Annual Reviews
Published: 2007-11-01
Volume: 23
Issue: 1
Pages: 519-547
ISSN: 1081-0706 (ISSN-L)
1530-8995
DOI: 10.1146/annurev.cellbio.23.090506.123319
PMC: PMC2911632
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: green
www.ncbi.nlm.nih.gov
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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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