Evolution and assembly of ESCRTs
Abstract
The AAA (ATPase associated with various cellular activities) proteins participate in membrane trafficking, organelle biogenesis, DNA replication, intracellular locomotion, cytoskeletal remodelling, protein folding and proteolysis. The AAA Vps (vacuolar protein sorting) 4 is central to traffic to lysosomes, retroviral budding and mammalian cell division. It dissociates ESCRTs (endosomal sorting complexes required for transport) from endosomal membranes, enabling their recycling to the cytosol, and plays a role in fission of intraluminal vesicles within MVBs (multivesicular bodies). The mechanism of Vps4-catalysed disassembly of ESCRT networks is unknown; however, it requires interaction between Vps4 and ESCRT-III subunits. The 30 C-terminal residues of Vps2 and Vps46 (Did2) subunits are both necessary and sufficient for interaction with the Vps4 N-terminal MIT (microtubule-interacting and transport) domain, and the crystal structure of the Vps2 C-terminus in a complex with the Vps4 MIT domain shows that MIT helices α2 and α3 recognize a (D/E)XXLXXRLXXL(K/R) MIM (MIT-interacting motif). These Vps2–MIT interactions are essential for vacuolar sorting and for Vps4-catalysed disassembly of ESCRT-III networks in vitro. Electron microscopy of ESCRT-III filaments assembled in vitro has enabled us to identify surfaces of the Vps24 subunit that are critical for protein sorting in vivo. The ESCRT-III–Vps4 interaction predates the divergence of Archaea and Eukarya. The Crenarchaea have three classes of ESCRT-III-like subunits, and one of these subunits interacts with an archaeal Vps4-like protein in a manner closely related to the human Vps4–human ESCRT-III subunit Vps20 interaction. This archaeal Vps4–ESCRT-III interaction appears to have a fundamental role in cell division in the Crenarchaea.
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CHMP2B is a subunit of the endosomal sorting complex required for transport-III (ESCRT-III).
“CHMP2B (charged multivesicular body protein 2B) is a subunit of the endosomal sorting complex required for transport-III (ESCRT-III) [262].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [262]
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- Authors
- Ghazi-Tabatabai, S., Obita, T., Pobbati, A. V., Perisic, O., Samson, R. Y., Bell, S. D., & Williams, R. L.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
- University of Oxford (GB)
- Corresponding author
- Obita, Takayuki
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2009-01-20
- Volume
- 37
- Issue
- 1
- Pages
- 151-155
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W1965914003
- Cited by
- 27
- References
- 36
- Citations by year
- 2026: 2 · 2021: 3 · 2019: 1 · 2016: 2 · 2015: 2 · 2013: 1 · 2012: 5
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (083639/Z/07/Z)
- 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, ESCRT-III, MIT domain, protein-protein interaction, multivesicular bodies, membrane trafficking, crenarchaeon, cell division
- MeSH terms
- Amino Acid Sequence, Humans, Molecular Sequence Data, Protein Binding, Endosomes, Saccharomyces cerevisiae, Evolution, Molecular, Protein Transport, Saccharomyces cerevisiae Proteins, Multiprotein Complexes
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