title: MIT domainia.
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.
authors.affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, MD 20892, USA. hurley@helix.nih.gov
authors.forename: James H
authors.initials: JH
authors.lastname: Hurley
authors.forename: Dong
authors.initials: D
authors.lastname: Yang
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D056827:Endosomal Sorting Complexes Required for Transport; D008954:Models, Biological; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000378:metabolism; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D025801:Ubiquitin / Q000378:metabolism; D033921:Vesicular Transport Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D056827:Endosomal Sorting Complexes Required for Transport; D010716:Phosphatidylinositols; D029701:Saccharomyces cerevisiae Proteins; D025801:Ubiquitin; C107528:VPS4 protein, S cerevisiae; C487285:VTA1 protein, S cerevisiae; D033921:Vesicular Transport Proteins; D000251:Adenosine Triphosphatases