ArticleNature structural & molecular biology2025
Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Molecular Mechanism of the SepF N‑Terminal Conformational Switch in Ring Assembly and Membrane Anchoring.JACS Au · 2026Article
- Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026Review
- Article
- Functional reconstitution of bacterial ESCRT-III protein PspA identifies key regions in membrane binding and remodeling.Protein science : a publication of the Protein Society · 2025Article
- The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- Beyond rings and rods: In-situ imaging reveals the role of VIPP1 in chloroplast homeostasis in tobacco.Plant physiology · 2025Article
- Asgard archaea reveal the conserved principles of ESCRT-III membrane remodeling.Science advances · 2025Article
- The Asgard archaeal ESCRT-III system forms helical filaments and remodels eukaryotic-like membranes.The EMBO journal · 2025Article
- Article
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Authors and funding
9 authors.
Funding
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Abstract
Eukaryotic members of the endosome sorting complex required for transport-III (ESCRT-III) family have been shown to form diverse higher-order assemblies. The bacterial phage shock protein A (PspA) has been identified as a member of the ESCRT-III superfamily, and PspA homo-oligomerizes to form rod-shaped assemblies. As observed for eukaryotic ESCRT-III, PspA forms tubular assemblies of varying diameters. Using electron cryo-electron microscopy, we determined 61 Synechocystis PspA structures and observed in molecular detail how the structural plasticity of PspA rods is mediated by conformational changes at three hinge regions in the monomer and by the fixed and changing molecular contacts between protomers. Moreover, we reduced and increased the structural plasticity of PspA rods by removing the loop connecting helices α3/α4 and the addition of nucleotides, respectively. Based on our analysis of PspA-mediated membrane remodeling, we suggest that the observed mode of structural plasticity is a prerequisite for the biological function of ESCRT-III members.
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