The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids
Open accessAbstract
The mitochondrial outer membrane protein, Mmm1p, is required for normal mitochondrial shape in yeast. To identify new morphology proteins, we isolated mutations incompatible with the mmm1-1 mutant. One of these mutants, mmm2-1, is defective in a novel outer membrane protein. Lack of Mmm2p causes a defect in mitochondrial shape and loss of mitochondrial DNA (mtDNA) nucleoids. Like the Mmm1 protein (Aiken Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. J. Cell Biol. 152:401-410.), Mmm2p is located in dot-like particles on the mitochondrial surface, many of which are adjacent to mtDNA nucleoids. While some of the Mmm2p-containing spots colocalize with those containing Mmm1p, at least some of Mmm2p is separate from Mmm1p. Moreover, while Mmm2p and Mmm1p both appear to be part of large complexes, we find that Mmm2p and Mmm1p do not stably interact and appear to be members of two different structures. We speculate that Mmm2p and Mmm1p are components of independent machinery, whose dynamic interactions are required to maintain mitochondrial shape and mtDNA structure.
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“In particular, deletion mutants of the ERMES core complex display defects in the segregation of mtDNA into daughter cells, resulting in the loss of mitochondria over several generations of growth in S. cerevisiae [27,29,30,45].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [30]
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Metadata
- Authors
- Youngman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E.
- Affiliations
- Johns Hopkins University (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-02-23
- Volume
- 164
- Issue
- 5
- Pages
- 677-688
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172170
- OpenAlex
- W1964155535
- Cited by
- 148
- References
- 53
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 3 · 2018: 8 · 2017: 8 · 2016: 12 · 2015: 4 · 2014: 15 · 2013: 7 · 2012: 5
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM054021, T32GM007445, R01-GM54021, 2T32-GM07445)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- mitochondrial outer membrane proteins, mitochondrial morphology, mtDNA maintenance, Saccharomyces cerevisiae, protein-protein interaction, protein complex structure
- MeSH terms
- Cell Division, Cell Membrane, DNA, Mitochondrial, Membrane Proteins, Mitochondria, Nucleic Acid Conformation, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Subcellular Fractions, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Macromolecular Substances
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