Abstract
The AAA ATPase Vps4 disassembles the membrane-bound ESCRT-III lattice. Four recent publications show how Vps4 carries out this task in a partnership with another ESCRT-associated protein, Vta1. Vps4 and Vta1 both contain MIT domains, which bind to "MIT-interacting motifs" (MIMs) of ESCRT-III proteins. As new MIT domain proteins are rapidly being identified, these studies will likely have relevance well beyond Vps4.
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / metabolism*
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Binding Sites
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Endosomal Sorting Complexes Required for Transport
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Models, Biological
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Models, Molecular
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Phosphatidylinositols / metabolism
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Protein Conformation
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / metabolism
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Ubiquitin / metabolism
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Vesicular Transport Proteins / chemistry
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Vesicular Transport Proteins / metabolism
Substances
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Endosomal Sorting Complexes Required for Transport
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Phosphatidylinositols
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Saccharomyces cerevisiae Proteins
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Ubiquitin
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VPS4 protein, S cerevisiae
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VTA1 protein, S cerevisiae
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Vesicular Transport Proteins
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Adenosine Triphosphatases