Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes
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- John McCullough
- Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112, USA;
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- Adam Frost
- Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158, USA
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- Wesley I. Sundquist
- Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112, USA;
書誌事項
- 公開日
- 2018-10-06
- DOI
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- 10.1146/annurev-cellbio-100616-060600
- 公開者
- Annual Reviews
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説明
<jats:p> The endosomal sorting complexes required for transport (ESCRT) pathway mediates cellular membrane remodeling and fission reactions. The pathway comprises five core complexes: ALIX, ESCRT-I, ESCRT-II, ESCRT-III, and Vps4. These soluble complexes are typically recruited to target membranes by site-specific adaptors that bind one or both of the early-acting ESCRT factors: ALIX and ESCRT-I/ESCRT-II. These factors, in turn, nucleate assembly of ESCRT-III subunits into membrane-bound filaments that recruit the AAA ATPase Vps4. Together, ESCRT-III filaments and Vps4 remodel and sever membranes. Here, we review recent advances in our understanding of the structures, activities, and mechanisms of the ESCRT-III and Vps4 machinery, including the first high-resolution structures of ESCRT-III filaments, the assembled Vps4 enzyme in complex with an ESCRT-III substrate, the discovery that ESCRT-III/Vps4 complexes can promote both inside-out and outside-in membrane fission reactions, and emerging mechanistic models for ESCRT-mediated membrane fission. </jats:p>
収録刊行物
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- Annual Review of Cell and Developmental Biology
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Annual Review of Cell and Developmental Biology 34 (1), 85-109, 2018-10-06
Annual Reviews