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Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance
Mitochondrial transport and anchoring mechanisms work in concert to position mitochondria to meet cellular needs. In yeast, Mmr1 functions as a mitochondrial adaptor for Myo2 to facilitate actin-based transport of mitochondria to the bud. Posttransport, Mmr1 is proposed to anchor mitochondria at the...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6249809/ https://www.ncbi.nlm.nih.gov/pubmed/30044712 http://dx.doi.org/10.1091/mbc.E18-02-0122 |
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author | Chen, WeiTing Ping, Holly A. Lackner, Laura L. |
author_facet | Chen, WeiTing Ping, Holly A. Lackner, Laura L. |
author_sort | Chen, WeiTing |
collection | PubMed |
description | Mitochondrial transport and anchoring mechanisms work in concert to position mitochondria to meet cellular needs. In yeast, Mmr1 functions as a mitochondrial adaptor for Myo2 to facilitate actin-based transport of mitochondria to the bud. Posttransport, Mmr1 is proposed to anchor mitochondria at the bud tip. Although both functions require an interaction between Mmr1 and mitochondria, the molecular basis of the Mmr1–mitochondria interaction is poorly understood. Our in vitro phospholipid binding assays indicate Mmr1 can directly interact with phospholipid membranes. Through structure–function studies we identified an unpredicted membrane-binding domain composed of amino acids 76–195 that is both necessary and sufficient for Mmr1 to interact with mitochondria in vivo and liposomes in vitro. In addition, our structure–function analyses indicate that the coiled-coil domain of Mmr1 is necessary and sufficient for Mmr1 self-interaction and facilitates the polarized localization of the protein. Disrupting either the Mmr1–membrane interaction or Mmr1 self-interaction leads to defects in mitochondrial inheritance. Therefore, direct membrane binding and self-interaction are necessary for Mmr1 function in mitochondrial inheritance and are utilized as a means to spatially and temporally regulate mitochondrial positioning. |
format | Online Article Text |
id | pubmed-6249809 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-62498092018-11-30 Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance Chen, WeiTing Ping, Holly A. Lackner, Laura L. Mol Biol Cell Articles Mitochondrial transport and anchoring mechanisms work in concert to position mitochondria to meet cellular needs. In yeast, Mmr1 functions as a mitochondrial adaptor for Myo2 to facilitate actin-based transport of mitochondria to the bud. Posttransport, Mmr1 is proposed to anchor mitochondria at the bud tip. Although both functions require an interaction between Mmr1 and mitochondria, the molecular basis of the Mmr1–mitochondria interaction is poorly understood. Our in vitro phospholipid binding assays indicate Mmr1 can directly interact with phospholipid membranes. Through structure–function studies we identified an unpredicted membrane-binding domain composed of amino acids 76–195 that is both necessary and sufficient for Mmr1 to interact with mitochondria in vivo and liposomes in vitro. In addition, our structure–function analyses indicate that the coiled-coil domain of Mmr1 is necessary and sufficient for Mmr1 self-interaction and facilitates the polarized localization of the protein. Disrupting either the Mmr1–membrane interaction or Mmr1 self-interaction leads to defects in mitochondrial inheritance. Therefore, direct membrane binding and self-interaction are necessary for Mmr1 function in mitochondrial inheritance and are utilized as a means to spatially and temporally regulate mitochondrial positioning. The American Society for Cell Biology 2018-09-15 /pmc/articles/PMC6249809/ /pubmed/30044712 http://dx.doi.org/10.1091/mbc.E18-02-0122 Text en © 2018 Chen et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License. |
spellingShingle | Articles Chen, WeiTing Ping, Holly A. Lackner, Laura L. Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title | Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title_full | Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title_fullStr | Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title_full_unstemmed | Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title_short | Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance |
title_sort | direct membrane binding and self-interaction contribute to mmr1 function in mitochondrial inheritance |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6249809/ https://www.ncbi.nlm.nih.gov/pubmed/30044712 http://dx.doi.org/10.1091/mbc.E18-02-0122 |
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