The DOI matches its Crossref record; 154 of the 154 references it cites were found in a registry or an index.
Biogenesis and Function of Multivesicular Bodies
Open accessAbstract
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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“For instance, actin-myosin interactions appear critical to the formation of all four types of EVs [66, 85, 100, 115].”
From Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013) · cites this paper as [115]
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Metadata
- Authors
- Piper, R. C., & Katzmann, D. J.
- Affiliations
- University of Iowa (US)
- Mayo Clinic (US)
- 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
- 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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