Regulators of Vps4 ATPase Activity at Endosomes Differentially Influence the Size and Rate of Formation of Intralumenal Vesicles
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Recruitment of endosomal sorting complexes required for transport (ESCRTs) to the cytosolic face of endosomes regulates selective inclusion of transmembrane proteins into the lumenal vesicles of multivesicular bodies (MVBs). ESCRT-0, -I, and -II bind directly to ubiquitinated transmembrane cargoes of the MVB pathway, whereas polymerization of ESCRT-III at endosomes is thought to bend the membrane and/or provide the energetic force that drives membrane scission and detachment of vesicles into the endosome lumen. Disassembly of the ESCRT-III polymer and dissociation of its subunits from endosomes requires the Vps4 ATPase, the activity of which is controlled in vivo by regulatory proteins. We identify distinct spatiotemporal roles for Vps4-regulating proteins through examinations of subcellular localization and endosome morphology. Did2 plays a unique role in the regulation of MVB lumenal vesicle size, whereas Vtal and Vps60 promote efficient membrane scission and delivery of membrane to the endosome lumen. These morphological effects probably result from Vps4-mediated manipulations of ESCRT-III, because we show dissociation of ESCRT-0, -I, and -II from endosomes is not directly dependent on Vps4 activity.
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ILV formation requires two distinct processes: organization of the endosome membrane into tetraspanin-enriched microdomains (TEMs) and ESCRT complexes.
“Work in yeast [28-31] and other tissue culture models [32-34] suggests that ILV formation requires two distinct processes. The first involves the organization of the endosome membrane into specialized units highly enriched for a class of membrane proteins called tetraspanins [35].”
From Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013) · cites this paper as [30]
The Introduction (page unavailable) says ESCRT complexes mediate packaging into intralumenal vesicles, supporting the ESCRT part of the claim. Our copy does not describe tetraspanin-enriched microdomains or establish that ILV formation requires the two distinct processes claimed. In the citing sentence, the tetraspanin-specific statement is separately cited to [35]. (LLM, conf=0.87)
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- Authors
- Nickerson, D. P., West, M., Henry, R., & Odorizzi, G.
- Affiliations
- University of Colorado Boulder (US)
- Corresponding author
- Odorizzi, Greg
- Venue
- Molecular Biology of the Cell
- Published
- 2010-03-15
- Volume
- 21
- Issue
- 6
- Pages
- 1023-1032
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2836955
- OpenAlex
- W2161384755
- Cited by
- 86
- References
- 57
- Citations by year
- 2025: 6 · 2023: 3 · 2022: 5 · 2021: 5 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 7 · 2014: 8 · 2013: 5 · 2012: 9
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Washington
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM065505, GM065505)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- ESCRT machinery, multivesicular bodies, vesicle size, membrane fission, endosomal sorting
- MeSH terms
- Adenosine Triphosphatases, Phenotype, Endosomes, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Multivesicular Bodies
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