ArticleNature communications2025
Structures of human organellar SPFH protein complexes.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A novel small-molecule inhibitor TD6 targets prohibitin 1 (PHB1) and suppresses colorectal cancer pulmonary metastasis by destabilizing mitochondrial complex I.Redox biology · 2026Article
- Addendum: In situ architecture of the human prohibitin complex.Nature cell biology · 2026Article
- N-glycosylation of ERLIN2 promotes hepatocellular carcinoma progression by enhancing CCNB1 stability.Molecular and cellular biochemistry · 2026Article
- Structural basis for prohibitin-mediated regulation of mitochondrial m-AAA protease.Nature communications · 2026Article
- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
- Article
- The vault associates with membranes in situ.Nature communications · 2026Article
- Structural plasticity of the membrane-bound protein degradation assembly supports bacterial adaptation to stress.Cell reports · 2026Article
- The vault particle is enclosed by aScience advances · 2026Article
- Molecular mechanisms of flotillin complexes in organizing membrane microdomains.Nature communications · 2026Article
- Cryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps.Structure (London, England : 1993) · 2025Article
- In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) family proteins are found in all kingdoms of life and in multiple eukaryotic organelles. SPFH proteins assemble into homo- or hetero-oligomeric rings that form domed structures. Most SPFH assemblies also abut a cellular membrane, where they are implicated in diverse functions ranging from membrane organization to protein quality control. However, the precise architectures of different SPFH complexes remain unclear. Here, we report single-particle cryo-EM structures of the endoplasmic reticulum (ER)-resident Erlin1/2 complex and the mitochondrial prohibitin (PHB1/2) complex, revealing assemblies of 13 heterodimers of Erlin1 and Erlin2 and 11 heterodimers of PHB1 and PHB2, respectively. We also describe key interactions underlying the architecture of each complex and conformational heterogeneity of the PHB1/2 complex. Our findings elucidate the distinct stoichiometries and properties of human organellar SPFH complexes and highlight common principles of SPFH complex organization.
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