ReviewJournal of molecular biology2016
Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.
Review in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 68 citations in OpenAlex.
- The Roles of Alix and VPS4A in Autophagy and Endosomal Pathways and Their Relation to HBV Replication.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Divergent functions of late ESCRT components in Giardia lamblia: Insights from subcellular distributions and protein interactions.PLoS neglected tropical diseases · 2025Article
- Substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.Scientific reports · 2025Article
- USP8 promotes intracellular infection by enhancing ESCRT-mediated membrane repair, limiting xenophagy, and reducing oxidative stress.Autophagy · 2025Article
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- The Roles of Exosomal Proteins: Classification, Function, and Applications.International journal of molecular sciences · 2023Review
- The role of Vps4 in cancer development.Frontiers in oncology · 2023Review
- ATP-binding and hydrolysis of human NLRP3.Communications biology · 2022Article
- Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Exploring the Effect of Mechanical Anisotropy of Protein Structures in the Unfoldase Mechanism of AAA+ Molecular Machines.Nanomaterials (Basel, Switzerland) · 2022Article
- Simulating the directional translocation of a substrate by the AAA+ motor in the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021Review
- Article
- Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.eLife · 2020Article
- Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.The Journal of biological chemistry · 2020Article
- A Structural View on ESCRT-Mediated Abscission.Frontiers in cell and developmental biology · 2020Review
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- Sorting out how Msp1 maintains mitochondrial membrane proteostasis.Mitochondrion · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Meiotic clade AAA ATPases (ATPases associated with diverse cellular activities), which were initially grouped on the basis of phylogenetic classification of their AAA ATPase cassette, include four relatively well characterized family members, Vps4, spastin, katanin and fidgetin. These enzymes all function to disassemble specific polymeric protein structures, with Vps4 disassembling the ESCRT-III polymers that are central to the many membrane-remodeling activities of the ESCRT (endosomal sorting complexes required for transport) pathway and spastin, katanin p60 and fidgetin affecting multiple aspects of cellular dynamics by severing microtubules. They share a common domain architecture that features an N-terminal MIT (microtubule interacting and trafficking) domain followed by a single AAA ATPase cassette. Meiotic clade AAA ATPases function as hexamers that can cycle between the active assembly and inactive monomers/dimers in a regulated process, and they appear to disassemble their polymeric substrates by translocating subunits through the central pore of their hexameric ring. Recent studies with Vps4 have shown that nucleotide-induced asymmetry is a requirement for substrate binding to the pore loops and that recruitment to the protein lattice via MIT domains also relieves autoinhibition and primes the AAA ATPase cassettes for substrate binding. The most striking, unifying feature of meiotic clade AAA ATPases may be their MIT domain, which is a module that is found in a wide variety of proteins that localize to ESCRT-III polymers. Spastin also displays an adjacent microtubule binding sequence, and the presence of both ESCRT-III and microtubule binding elements may underlie the recent findings that the ESCRT-III disassembly function of Vps4 and the microtubule-severing function of spastin, as well as potentially katanin and fidgetin, are highly coordinated.
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Registered trials
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.