The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Formation of Membrane-bound Ring Complexes by Prohibitins in Mitochondria
Open accessAbstract
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 ∼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 ∼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 ∼270 × 200 Å. Implications of these findings for proposed cellular activities of prohibitins are discussed.
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A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
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Metadata
- Authors
- Tatsuta, T., Model, K., & Langer, T.
- Venue
- Molecular Biology of the Cell
- Published
- 2005-01
- Volume
- 16
- Issue
- 1
- Pages
- 248-259
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2108560778
- Cited by
- 344
- References
- 39
- FWCI
- 3.39
- Type
- journal article
- Language
- en
- Open access
- green
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