VPS4 Antibody

1. The authors now report a 3.2 A structure of Vps4 bound to an ESCRT-III peptide substrate. The new structure reveals that the peptide approximates a beta-strand conformation whose helical symmetry matches that of the five Vps4 subunits it contacts directly. PMID: 29165244
2. The authors propose a model in which multiple Vps4 hexamers (four or more) draw together several ESCRT-III filaments. This process induces cargo crowding and inward membrane buckling, followed by constriction of the nascent bud neck and ultimately intraluminal vesicle generation by vesicle fission. PMID: 29019322
3. These data support a mechanism in which Vps4 disassembles its substrates by completely unfolding them and threading them through the central pore. PMID: 25938660
4. Data implicate the ESCRT machinery in preventing the formation of nonfunctional nuclear pore complexes (NPCs); authors propose a model in which ESCRT-III/Vps4 helps recognize and clear defective NPC assembly intermediates before a step in which they are committed to maturing into a malformed NPC destined for the storage of improperly assembled nuclear pore complexes compar PMID: 25303532
5. Vfa1 is a novel positive regulator of Vps4 function PMID: 24567329
6. analysis of the Vps4 AAA ATPase linker region, which plays a regulatory role in assembly and activity PMID: 23913684
7. Results identify distinct spatiotemporal roles for Vps4-regulating proteins through examinations of subcellular localization and endosome morphology. PMID: 20089837
8. Results present a systematic in vivo analysis of the Vps4 interaction network. PMID: 20110351
9. Assembly of a Vps4p oligomeric complex with full ATPase activity that interacts with Vta1p is essential for normal endosome function. PMID: 16704411
10. We determined the crystal structure of the Vps2 C terminus in a complex with the Vps4 MIT domain, explaining the basis for selective ESCRT-III recognition PMID: 17928861
11. Vps4 functions in the MVB pathway via a highly conserved mechanism supported by similar protein-protein interactions during its ATPase reaction cycle PMID: 17949747
12. The second region of homology (SRH) function of Vps4 requires an intact C-terminal helix and is important for assembly and intersubunit catalysis in AAA ATPases. PMID: 18266866
13. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head--not in a head-to-tail-fashion as in class II AAA-ATPases PMID: 18272179
14. ATP hydrolysis would eliminate this interaction and subsequent nucleotide release causes the domains to rotate, which together lead to the disassembly of the SKD1 oligomer PMID: 18796009
15. Mutational analyses demonstrate that pore loop 2 residues Arg241 and Arg251 are required for efficient HIV-1 budding, thereby supporting a role for this "arginine collar" in Vps4 function. PMID: 18929572

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KEGG: sce:YPR173C

STRING: 4932.YPR173C