ArticleThe Journal of cell biology2018
Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture.
Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Vps1 drives membrane constriction and fission necessary for endosomal protein sorting.The EMBO journal · 2026Article
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The dynamin-related protein Vps1 and the peroxisomal membrane protein Pex27 function together during peroxisome fission.Journal of cell science · 2023Article
- Toxicity and assimilation of cellulosic copper nanoparticles require α-arrestins in S. cerevisiae.Metallomics : integrated biometal science · 2023Article
- Light Scattering Techniques to Assess Self-Assembly and Hydrodynamics of Membrane Trafficking Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- Structural and functional characterization of the dominant negative P-loop lysine mutation in the dynamin superfamily protein Vps1.Protein science : a publication of the Protein Society · 2020Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Article
- Ivy1 is a negative regulator of Gtr-dependent TORC1 activation.Journal of cell science · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Dynamin-related proteins (DRPs) are large multidomain GTPases required for diverse membrane-remodeling events. DRPs self-assemble into helical structures, but how these structures are tailored to their cellular targets remains unclear. We demonstrate that the fungal DRP Vps1 primarily localizes to and functions at the endosomal compartment. We present crystal structures of a Vps1 GTPase-bundle signaling element (BSE) fusion in different nucleotide states to capture GTP hydrolysis intermediates and concomitant conformational changes. Using cryoEM, we determined the structure of full-length GMPPCP-bound Vps1. The Vps1 helix is more open and flexible than that of dynamin. This is due to further opening of the BSEs away from the GTPase domains. A novel interface between adjacent GTPase domains forms in Vps1 instead of the contacts between the BSE and adjacent stalks and GTPase domains as seen in dynamin. Disruption of this interface abolishes Vps1 function in vivo. Hence, Vps1 exhibits a unique helical architecture, highlighting structural flexibilities of DRP self-assembly.
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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.