MMM1 Encodes a Mitochondrial Outer Membrane Protein Essential for Establishing and Maintaining the Structure of Yeast Mitochondria
Open accessAbstract
In the yeast Saccharomyces cerevisiae, mitochondria are elongated organelles which form a reticulum around the cell periphery. To determine the mechanism by which mitochondrial shape is established and maintained, we screened yeast mutants for those defective in mitochondrial morphology. One of these mutants, mmm1, is temperature-sensitive for the external shape of its mitochondria. At the restrictive temperature, elongated mitochondria appear to quickly collapse into large, spherical organelles. Upon return to the permissive temperature, wild-type mitochondrial structure is restored. The morphology of other cellular organelles is not affected in mmm1 mutants, and mmm1 does not disrupt normal actin or tubulin organization. Cells disrupted in the MMM1 gene are inviable when grown on nonfermentable carbon sources and show abnormal mitochondrial morphology at all temperatures. The lethality of mmm1 mutants appears to result from the inability to segregate the aberrant-shaped mitochondria into daughter cells. Mitochondrial structure is therefore important for normal cell function. Mmm1p is located in the mitochondrial outer membrane, with a large carboxyl-terminal domain facing the cytosol. We propose that Mmm1p maintains mitochondria in an elongated shape by attaching the mitochondrion to an external framework, such as the cytoskeleton.
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The ERMES complex is involved in mitochondrial fission, the distribution of mtDNA, and mitophagy.
“The ERMES complex is also involved in mitochondrial fission, the distribution of mtDNA, and mitophagy [27,28,29,30,31,32,33].”
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 [28]
The Results (pp. 1378, 1386–1387) show that MMM1 mutants have altered mitochondrial shape and impaired transmission of DNA-containing mitochondria to daughter buds. The Discussion raises mitochondrial division as a possible mechanism but does not establish a role in fission. Our copy does not discuss the ERMES complex or mitophagy, or directly establish a role in mtDNA distribution. (LLM, conf=0.84)
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- Authors
- Burgess, S. M., Delannoy, M., & Jensen, R. E.
- Affiliations
- Johns Hopkins University (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1994-09-15
- Volume
- 126
- Issue
- 6
- Pages
- 1375-1391
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2290956
- OpenAlex
- W2166125801
- Cited by
- 249
- References
- 72
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 7 · 2023: 6 · 2022: 3 · 2021: 6 · 2020: 8 · 2019: 3 · 2018: 4 · 2017: 9 · 2016: 10 · 2015: 8 · 2014: 10 · 2013: 7 · 2012: 6
- FWCI
- 3.80
- 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)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (5T32GN07445)
- National Institute of General Medical Sciences (R01GM46803, R01GM046803)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial outer membrane proteins, mitochondrial morphology, Saccharomyces cerevisiae, temperature-sensitive mutants, mitochondrial segregation, organelle structure
- MeSH terms
- Amino Acid Sequence, Base Sequence, Carbon, Cell Membrane Permeability, Fungal Proteins, Genes, Fungal, Intracellular Membranes, Membrane Proteins, Mitochondria, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Temperature, Saccharomyces cerevisiae Proteins
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