ArticleThe Journal of biological chemistry2015
Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Assembly and priming of the VPS4B AAA+ ATPase of the human ESCRT system.Research square · 2026Article
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026Review
- Substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.Scientific reports · 2025Article
- ESCRT-III: a versatile membrane remodeling machinery and its implications in cellular processes and diseases.Animal cells and systems · 2024Review
- The precise function of alphaherpesvirus tegument proteins and their interactions during the viral life cycle.Frontiers in microbiology · 2024Review
- Article
- An ESCRT/VPS4 Envelopment Trap To Examine the Mechanism of Alphaherpesvirus Assembly and Transport in Neurons.Journal of virology · 2022Article
- Article
- Spastin recovery in hereditary spastic paraplegia by preventing neddylation-dependent degradation.Life science alliance · 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
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structure of the Cdc48 segregase in the act of unfolding an authentic substrate.Science (New York, N.Y.) · 2019Article
- Seeking Closure: How Do Herpesviruses Recruit the Cellular ESCRT Apparatus?Journal of virology · 2019Review
- Article
- Article
- Recent progress in the emerging role of exosome in hepatocellular carcinoma.Cell proliferation · 2019Review
- Structure and mechanism of the ESCRT pathway AAA+ ATPase Vps4.Biochemical Society transactions · 2019Review
- Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes.Annual review of cell and developmental biology · 2018Review
- Dividing the Archaeal Way: The Ancient Cdv Cell-Division Machinery.Frontiers in microbiology · 2018Review
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Authors and funding
6 authors.
Funding
Abstract
The endosomal sorting complexes required for transport (ESCRT) pathway drives reverse topology membrane fission events within multiple cellular pathways, including cytokinesis, multivesicular body biogenesis, repair of the plasma membrane, nuclear membrane vesicle formation, and HIV budding. The AAA ATPase Vps4 is recruited to membrane necks shortly before fission, where it catalyzes disassembly of the ESCRT-III lattice. The N-terminal Vps4 microtubule-interacting and trafficking (MIT) domains initially bind the C-terminal MIT-interacting motifs (MIMs) of ESCRT-III subunits, but it is unclear how the enzyme then remodels these substrates in response to ATP hydrolysis. Here, we report quantitative binding studies that demonstrate that residues from helix 5 of the Vps2p subunit of ESCRT-III bind to the central pore of an asymmetric Vps4p hexamer in a manner that is dependent upon the presence of flexible nucleotide analogs that can mimic multiple states in the ATP hydrolysis cycle. We also find that substrate engagement is autoinhibited by the Vps4p MIT domain and that this inhibition is relieved by binding of either Type 1 or Type 2 MIM elements, which bind the Vps4p MIT domain through different interfaces. These observations support the model that Vps4 substrates are initially recruited by an MIM-MIT interaction that activates the Vps4 central pore to engage substrates and generate force, thereby triggering ESCRT-III disassembly.
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