ArticleThe Journal of biological chemistry2015
A novel mechanism of regulating the ATPase VPS4 by its cofactor LIP5 and the endosomal sorting complex required for transport (ESCRT)-III protein CHMP5.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026Review
- Article
- Coordination of the host Vps4-Vta1 complex and the viral core protein Ac93 facilitates entry of Autographa californica multiple nucleopolyhedrovirus budded virions.Journal of virology · 2025Article
- Shining the light on mesenchymal stem cell-derived exosomes in breast cancer.Stem cell research & therapy · 2023Review
- LIP5, a MVB biogenesis regulator, is required for rice growth.Frontiers in plant science · 2023Article
- Proteomic analysis of diabetic retinas.Frontiers in endocrinology · 2023Article
- Article
- 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
- Mechanism of cargo sorting into small extracellular vesicles.Bioengineered · 2021Article
- The ESCRT-III molecules regulate the apical targeting of bile salt export pump.Journal of biomedical science · 2021Article
- Structural Insights into AQP2 Targeting to Multivesicular Bodies.International journal of molecular sciences · 2019Article
- Plant and Mammal Aquaporins: Same but Different.International journal of molecular sciences · 2018Review
- Aquaporin Protein-Protein Interactions.International journal of molecular sciences · 2017Review
- Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.The Journal of biological chemistry · 2017Article
- Identification and Characterization of BmVta1, a Bombyx mori (Lepidoptera: Bombycidae) Homologue for Vta1 That is Up-Regulated in Development.Journal of insect science (Online) · 2017Article
- Article
- Insights into Thiol-Aromatic Interactions: A Stereoelectronic Basis for S-H/π Interactions.Journal of the American Chemical Society · 2017Article
- NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.Scientific reports · 2016Article
- 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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Disassembly of the endosomal sorting complex required for transport (ESCRT) machinery from biological membranes is a critical final step in cellular processes that require the ESCRT function. This reaction is catalyzed by VPS4, an AAA-ATPase whose activity is tightly regulated by a host of proteins, including LIP5 and the ESCRT-III proteins. Here, we present structural and functional analyses of molecular interactions between human VPS4, LIP5, and the ESCRT-III proteins. The N-terminal domain of LIP5 (LIP5NTD) is required for LIP5-mediated stimulation of VPS4, and the ESCRT-III protein CHMP5 strongly inhibits the stimulation. Both of these observations are distinct from what was previously described for homologous yeast proteins. The crystal structure of LIP5NTD in complex with the MIT (microtubule-interacting and transport)-interacting motifs of CHMP5 and a second ESCRT-III protein, CHMP1B, was determined at 1 Å resolution. It reveals an ESCRT-III binding induced moderate conformational change in LIP5NTD, which results from insertion of a conserved CHMP5 tyrosine residue (Tyr(182)) at the core of LIP5NTD structure. Mutation of Tyr(182) partially relieves the inhibition displayed by CHMP5. Together, these results suggest a novel mechanism of VPS4 regulation in metazoans, where CHMP5 functions as a negative allosteric switch to control LIP5-mediated stimulation of VPS4.
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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.