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Cited by 152Mitochondrial Function and PathologyAutophagy in Disease and TherapyFungal and yeast genetics research

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

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Youngman, Matthew J., Hobbs, Alyson E. Aiken, Burgess, Shawn M., Srinivasan, Maithreyan, Jensen, Robert E.·2004·The Journal of Cell Biology
DOI 10.1083/jcb.200308012PMC PMC2172170
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Abstract

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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  1. 1991, Mol. Cell. Biol., 11, 1295
  2. 1996, Biol. Chem., 377, 535
  3. 1987, J. Cell Sci., 88(Pt 4), 431
  4. 1949, Arch. Biochem., 22, 331
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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)
ORCID
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
DOI
10.1083/jcb.200308012
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
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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