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Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance
The Rab GTPase Ypt11 is a Myo2-binding protein implicated in mother-to-bud transport of the cortical endoplasmic reticulum (ER), late Golgi, and mitochondria during yeast division. However, its reported subcellular localization does not reflect all of these functions. Here we show that Ypt11 is norm...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623639/ https://www.ncbi.nlm.nih.gov/pubmed/23427260 http://dx.doi.org/10.1091/mbc.E12-12-0848 |
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author | Lewandowska, Agnieszka Macfarlane, Jane Shaw, Janet M. |
author_facet | Lewandowska, Agnieszka Macfarlane, Jane Shaw, Janet M. |
author_sort | Lewandowska, Agnieszka |
collection | PubMed |
description | The Rab GTPase Ypt11 is a Myo2-binding protein implicated in mother-to-bud transport of the cortical endoplasmic reticulum (ER), late Golgi, and mitochondria during yeast division. However, its reported subcellular localization does not reflect all of these functions. Here we show that Ypt11 is normally a low-abundance protein whose ER localization is only detected when the protein is highly overexpressed. Although it has been suggested that ER-localized Ypt11 and ER–mitochondrial contact sites might mediate passive transport of mitochondria into the bud, we found that mitochondrial, but not ER, association is essential for Ypt11 function in mitochondrial inheritance. Our studies also reveal that Ypt11 function is regulated at multiple levels. In addition to membrane targeting and GTPase domain–dependent effector interactions, the abundance of active Ypt11 forms is controlled by phosphorylation status and degradation. We present a model that synthesizes these new features of Ypt11 function and regulation in mitochondrial inheritance. |
format | Online Article Text |
id | pubmed-3623639 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36236392013-06-30 Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance Lewandowska, Agnieszka Macfarlane, Jane Shaw, Janet M. Mol Biol Cell Articles The Rab GTPase Ypt11 is a Myo2-binding protein implicated in mother-to-bud transport of the cortical endoplasmic reticulum (ER), late Golgi, and mitochondria during yeast division. However, its reported subcellular localization does not reflect all of these functions. Here we show that Ypt11 is normally a low-abundance protein whose ER localization is only detected when the protein is highly overexpressed. Although it has been suggested that ER-localized Ypt11 and ER–mitochondrial contact sites might mediate passive transport of mitochondria into the bud, we found that mitochondrial, but not ER, association is essential for Ypt11 function in mitochondrial inheritance. Our studies also reveal that Ypt11 function is regulated at multiple levels. In addition to membrane targeting and GTPase domain–dependent effector interactions, the abundance of active Ypt11 forms is controlled by phosphorylation status and degradation. We present a model that synthesizes these new features of Ypt11 function and regulation in mitochondrial inheritance. The American Society for Cell Biology 2013-04-15 /pmc/articles/PMC3623639/ /pubmed/23427260 http://dx.doi.org/10.1091/mbc.E12-12-0848 Text en © 2013 Lewandowska et al. 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 (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Lewandowska, Agnieszka Macfarlane, Jane Shaw, Janet M. Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title | Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title_full | Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title_fullStr | Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title_full_unstemmed | Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title_short | Mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active Rab GTPase Ypt11 for mitochondrial inheritance |
title_sort | mitochondrial association, protein phosphorylation, and degradation regulate the availability of the active rab gtpase ypt11 for mitochondrial inheritance |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623639/ https://www.ncbi.nlm.nih.gov/pubmed/23427260 http://dx.doi.org/10.1091/mbc.E12-12-0848 |
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