ArticleJournal of molecular biology2014
The oligomeric state of the active Vps4 AAA ATPase.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 62 citations in OpenAlex.
- Assembly and priming of the VPS4B AAA+ ATPase of the human ESCRT system.Research square · 2026Article
- Identification of novel VPS4 inhibitors using multi-tiered structure based virtual screening.Molecular diversity · 2026Article
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026Review
- Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Cran1, member of a new class of OLD family ATPases, functions in cell cycle progression in an archaeon.EMBO reports · 2026Article
- Ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms from diverse species show differences in oligomeric structure, thermal stability, and activity.European biophysics journal : EBJ · 2025Article
- Substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.Scientific reports · 2025Article
- The green ESCRTs: Newly defined roles for ESCRT proteins in plants.The Journal of biological chemistry · 2025Review
- Defects in Exosome Biogenesis Are Associated with Sensorimotor Defects in ZebrafishThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- The human AAA-ATPase VPS4A isoform and its co-factor VTA1 have a unique function in regulating mammalian cytokinesis abscission.PLoS biology · 2024Article
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- Review
- The ESCRT System Plays an Important Role in the Germination in Candida albicans by Regulating the Expression of Hyphal-Specific Genes and the Localization of Polarity-Related Proteins.Mycopathologia · 2020Article
- Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.Communications biology · 2020Article
- A Structural View on ESCRT-Mediated Abscission.Frontiers in cell and developmental biology · 2020Review
- Article
- VPS4 triggers constriction and cleavage of ESCRT-III helical filaments.Science advances · 2019Article
- Structure and mechanism of the ESCRT pathway AAA+ ATPase Vps4.Biochemical Society transactions · 2019Review
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
- Endosomal trafficking of yeast membrane proteins.Biochemical Society transactions · 2018Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The cellular ESCRT (endosomal sorting complexes required for transport) pathway drives membrane constriction toward the cytosol and effects membrane fission during cytokinesis, endosomal sorting, and the release of many enveloped viruses, including the human immunodeficiency virus. A component of this pathway, the AAA ATPase Vps4, provides energy for pathway progression. Although it is established that Vps4 functions as an oligomer, subunit stoichiometry and other fundamental features of the functional enzyme are unclear. Here, we report that although some mutant Vps4 proteins form dodecameric assemblies, active wild-type Saccharomyces cerevisiae and Sulfolobus solfataricus Vps4 enzymes can form hexamers in the presence of ATP and ADP, as assayed by size-exclusion chromatography and equilibrium analytical ultracentrifugation. The Vta1p activator binds hexameric yeast Vps4p without changing the oligomeric state of Vps4p, implying that the active Vta1p-Vps4p complex also contains a single hexameric ring. Additionally, we report crystal structures of two different archaeal Vps4 homologs, whose structures and lattice interactions suggest a conserved mode of oligomerization. Disruption of the proposed hexamerization interface by mutagenesis abolished the ATPase activity of archaeal Vps4 proteins and blocked Vps4p function in S. cerevisiae. These data challenge the prevailing model that active Vps4 is a double-ring dodecamer, and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six subunits.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.