ArticleMolecular biology of the cell2005
Formation of membrane-bound ring complexes by prohibitins in mitochondria.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
171 citing papers in PubMed, 345 citations in OpenAlex.
- Prohibitin controls MRS2-Mediated mitochondrial MgCell reports · 2026Article
- Prohibitin 2 is a key regulator of T cell proliferation, differentiation, and effector functions in vivo.Communications biology · 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
- Podocin oligomers regulate the ordering of nephrin chains, providing the molecular basis ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Estrogen-Induced Hypermethylation Silencing ofCells · 2026Article
- Prohibitins: emerging host targets of bacteria and viruses at the plasma membrane, mitochondria, and cytoplasm.Microbial cell (Graz, Austria) · 2026Article
- Structures of human organellar SPFH protein complexes.Nature communications · 2025Article
- Enhancing cross-organelle coordination to advance plant cytochrome P450 functionality in yeast.Science advances · 2025Article
- Cryo-EM structure of the prohibitin complex in open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for membrane microdomain formation by a human Stomatin complex.Nature communications · 2025Article
- The SPFH complex HflK-HflC regulates aerobic respiration in bacteria.PLoS biology · 2025Article
- Efficient PHB2 (prohibitin 2) exposure during mitophagy depends on VDAC1 (voltage dependent anion channel 1).Autophagy · 2025Article
- Prohibitins in infection: potential therapeutic targets.Future microbiology · 2025Review
- Proteolytic regulation of mitochondrial magnesium channel by m-AAA protease and prohibitin complex.Genetics · 2025Article
- Prohibitin 1 tethers lipid membranes and regulates OPA1-mediated membrane fusion.The Journal of biological chemistry · 2025Article
- Mitochondrial damage and IL-1β production in monocytes caused byFrontiers in immunology · 2025Article
- Article
- Non-cell autonomous regulation of cell-cell signaling and differentiation by mitochondrial ROS.The Journal of cell biology · 2024Article
- CRISPR-editing of the virus vectorMethodsX · 2024Article
111 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prohibitins comprise a remarkably conserved protein family in eukaryotic cells with proposed functions in cell cycle progression, senescence, apoptosis, and the regulation of mitochondrial activities. Two prohibitin homologues, Phb1 and Phb2, assemble into a high molecular weight complex of approximately 1.2 MDa in the mitochondrial inner membrane, but a nuclear localization of Phb1 and Phb2 also has been reported. Here, we have analyzed the biogenesis and structure of the prohibitin complex in Saccharomyces cerevisiae. Both Phb1 and Phb2 subunits are targeted to mitochondria by unconventional noncleavable targeting sequences at their amino terminal end. Membrane insertion involves binding of newly imported Phb1 to Tim8/13 complexes in the intermembrane space and is mediated by the TIM23-translocase. Assembly occurs via intermediate-sized complexes of approximately 120 kDa containing both Phb1 and Phb2. Conserved carboxy-terminal coiled-coil regions in both subunits mediate the formation of large assemblies in the inner membrane. Single particle electron microscopy of purified prohibitin complexes identifies diverse ring-shaped structures with outer dimensions of approximately 270 x 200 angstroms. Implications of these findings for proposed cellular activities of prohibitins are discussed.
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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.