Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
Open accessAbstract
Endosomal sorting complex required for transport III (ESCRT-III) proteins function in multivesicular body biogenesis and viral budding. They are recruited from the cytoplasm to the membrane, where they assemble into large complexes. We used “deep-etch” electron microscopy to examine polymers formed by the ESCRT-III proteins hSnf7-1 (CHMP4A) and hSnf7-2 (CHMP4B). When overexpressed, these proteins target to endosomes and the plasma membrane. Both hSnf7 proteins assemble into regular approximately 5-nm filaments that curve and self-associate to create circular arrays. Binding to a coexpressed adenosine triphosphate hydrolysis–deficient mutant of VPS4B draws these filaments together into tight circular scaffolds that bend the membrane away from the cytoplasm to form buds and tubules protruding from the cell surface. Similar buds develop in the absence of mutant VPS4B when hSnf7-1 is expressed without its regulatory C-terminal domain. We demonstrate that hSnf7 proteins form novel membrane-attached filaments that can promote or stabilize negative curvature and outward budding. We suggest that ESCRT-III polymers delineate and help generate the luminal vesicles of multivesicular bodies.
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Key ESCRT-III components, such as CHMP2 and CHMP4, and VPS4 ATPase, are recruited to the budding site at the plasma membrane.
“key ESCRT-III components, such as charged multivesicular body proteins 2 and 4 (CHMP2 and CHMP4), and the vacuolar protein sorting-associated protein 4 ATPase (VPS4 ATPase), are recruited to the budding site at the plasma membrane”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Hanson et al. 2008
The Results (page unavailable) show CHMP4 filaments and a coexpressed hydrolysis-defective VPS4B mutant at plasma-membrane arrays associated with buds. The Discussion (page unavailable) says ESCRT machinery, probably including ESCRT-III, is recruited to the plasma membrane. The paper does not establish that CHMP2 is recruited to those budding sites, and its direct budding-site observation uses mutant rather than unqualified VPS4. (LLM, conf=0.87)
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- Authors
- Hanson, P. I., Roth, R., Lin, Y., & Heuser, J. E.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-01-21
- Volume
- 180
- Issue
- 2
- Pages
- 389-402
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2213594
- OpenAlex
- W2166456692
- Cited by
- 427
- References
- 1
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- FWCI
- 21.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM029647)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- ESCRT-III, CHMP4A, CHMP4B, VPS4B, membrane curvature, plasma membrane deformation, multivesicular body biogenesis, viral budding, membrane budding, membrane tubules, protein polymers, endosomes
- MeSH terms
- Animals, Carrier Proteins, Cell Line, Cell Membrane, Chlorocebus aethiops, Humans, Microscopy, Electron, Mutation, Polymers, Endosomes, Transfection, COS Cells, Vesicular Transport Proteins, Endosomal Sorting Complexes Required for Transport
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