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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February 2009
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Conference Article|
January 20 2009
Evolution and assembly of ESCRTs
Sara Ghazi-Tabatabai;
Sara Ghazi-Tabatabai
*MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
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Takayuki Obita;
Takayuki Obita
*MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
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Ajaybabu V. Pobbati;
Ajaybabu V. Pobbati
*MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
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Olga Perisic;
Olga Perisic
*MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
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Rachel Y. Samson;
Rachel Y. Samson
†Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, U.K.
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Stephen D. Bell;
Stephen D. Bell
†Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, U.K.
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Roger L. Williams
Roger L. Williams
1
*MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, U.K.
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
November 17 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (1): 151–155.
Article history
Received:
November 17 2008
Citation
Sara Ghazi-Tabatabai, Takayuki Obita, Ajaybabu V. Pobbati, Olga Perisic, Rachel Y. Samson, Stephen D. Bell, Roger L. Williams; Evolution and assembly of ESCRTs. Biochem Soc Trans 1 February 2009; 37 (1): 151–155. doi: https://doi.org/10.1042/BST0370151
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