ArticleProtein science : a publication of the Protein Society2020
Structural and functional characterization of the dominant negative P-loop lysine mutation in the dynamin superfamily protein Vps1.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Upregulated small GTPase immunity-associated proteins confer resistance toFrontiers in cellular and infection microbiology · 2025Article
- The dynamin-related protein Vps1 and the peroxisomal membrane protein Pex27 function together during peroxisome fission.Journal of cell science · 2023Article
- A dominant negative mitofusin causes mitochondrial perinuclear clusters because of aberrant tethering.Life science alliance · 2023Article
- Light Scattering Techniques to Assess Self-Assembly and Hydrodynamics of Membrane Trafficking Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- 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
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Dynamin-superfamily proteins (DSPs) are large self-assembling mechanochemical GTPases that harness GTP hydrolysis to drive membrane remodeling events needed for many cellular processes. Mutation to alanine of a fully conserved lysine within the P-loop of the DSP GTPase domain results in abrogation of GTPase activity. This mutant has been widely used in the context of several DSPs as a dominant-negative to impair DSP-dependent processes. However, the precise deficit of the P-loop K to A mutation remains an open question. Here, we use biophysical, biochemical and structural approaches to characterize this mutant in the context of the endosomal DSP Vps1. We show that the Vps1 P-loop K to A mutant binds nucleotide with an affinity similar to wild type but exhibits defects in the organization of the GTPase active site that explain the lack of hydrolysis. In cells, Vps1 and Dnm1 bearing the P-loop K to A mutation are defective in disassembly. These mutants become trapped in assemblies at the typical site of action of the DSP. This work provides mechanistic insight into the widely-used DSP P-loop K to A mutation and the basis of its dominant-negative effects in the cell.
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