ArticleThe Journal of biological chemistry2014
Vps4 stimulatory element of the cofactor Vta1 contacts the ATPase Vps4 α7 and α9 to stimulate ATP hydrolysis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- Identification of novel VPS4 inhibitors using multi-tiered structure based virtual screening.Molecular diversity · 2026Article
- Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.Molecular biology of the cell · 2021Article
- Bro1 stimulates Vps4 to promote intralumenal vesicle formation during multivesicular body biogenesis.The Journal of cell biology · 2021Article
- Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.Cell reports · 2019Article
- Molecular switch-like regulation in motor proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.eLife · 2017Article
- Cryo-EM structures of the ATP-bound Vps4Nature communications · 2017Article
- Article
- Reverse-topology membrane scission by the ESCRT proteins.Nature reviews. Molecular cell biology · 2017Review
- Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.Journal of molecular biology · 2016Review
- Role of SKD1 Regulators LIP5 and IST1-LIKE1 in Endosomal Sorting and Plant Development.Plant physiology · 2016Article
- Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation.The Journal of biological chemistry · 2015Article
- Altered cofactor regulation with disease-associated p97/VCP mutations.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A novel mechanism of regulating the ATPase VPS4 by its cofactor LIP5 and the endosomal sorting complex required for transport (ESCRT)-III protein CHMP5.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The endosomal sorting complexes required for transport (ESCRTs) function in a variety of membrane remodeling processes including multivesicular body sorting, abscission during cytokinesis, budding of enveloped viruses, and repair of the plasma membrane. Vps4 ATPase activity modulates ESCRT function and is itself modulated by its cofactor Vta1 and its substrate ESCRT-III. The carboxyl-terminal Vta1/SBP-1/Lip5 (VSL) domain of Vta1 binds to the Vps4 β-domain to promote Vps4 oligomerization-dependent ATP hydrolysis. Additionally, the Vps4 stimulatory element (VSE) of Vta1 contributes to enhancing Vps4 oligomer ATP hydrolysis. The VSE is also required for Vta1-dependent stimulation of Vps4 by ESCRT-III subunits. However, the manner by which the Vta1 VSE contributes to Vps4 activation is unknown. Existing structural data were used to generate a model of the Vta1 VSE in complex with Vps4. This model implicated residues within the small ATPase associated with various activities (AAA) domain, specifically α-helices 7 and 9, as relevant contact sites. Rational generation of Vps4 mutants defective for VSE-mediated stimulation, as well as intergenic compensatory mutations, support the validity of this model. These findings have uncovered the Vps4 surface responsible for coordinating ESCRT-III-stimulated Vta1 input during ESCRT function and identified a novel mechanism of Vps4 stimulation.
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Registered trials
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