Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly

Summary: Dynamic processes such as fusion, fission, and trafficking are important in the regulation of cellular organelles, with an abundant literature focused on mitochondria. Mitochondrial dynamics not only help shape its network within cells but also are involved in the modulation of respiration...

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Main Authors: Ying-Chieh Chen, Tzu-Hao Cheng, Wei-Ling Lin, Chang-Lin Chen, Wei Yuan Yang, Craig Blackstone, Chuang-Rung Chang
Format: Article
Language:English
Published: Elsevier 2019-01-01
Series:iScience
Online Access:http://www.sciencedirect.com/science/article/pii/S2589004218302517
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author Ying-Chieh Chen
Tzu-Hao Cheng
Wei-Ling Lin
Chang-Lin Chen
Wei Yuan Yang
Craig Blackstone
Chuang-Rung Chang
author_facet Ying-Chieh Chen
Tzu-Hao Cheng
Wei-Ling Lin
Chang-Lin Chen
Wei Yuan Yang
Craig Blackstone
Chuang-Rung Chang
author_sort Ying-Chieh Chen
collection DOAJ
description Summary: Dynamic processes such as fusion, fission, and trafficking are important in the regulation of cellular organelles, with an abundant literature focused on mitochondria. Mitochondrial dynamics not only help shape its network within cells but also are involved in the modulation of respiration and integrity. Disruptions of mitochondrial dynamics are associated with neurodegenerative disorders. Although proteins that directly bind mitochondria to promote membrane fusion/fission have been studied intensively, machineries that regulate dynamic mitochondrial processes remain to be explored. We have identified an interaction between the mitochondrial fission GTPase Dnm1/DRP1 and the actin-regulatory protein Srv2/CAP at mitochondria. Deletion of Srv2 causes elongated-hyperfused mitochondria and reduces the reserved respiration capacity in yeast cells. Our results further demonstrate that the irregular network morphology in Δsrv2 cells derives from disrupted actin assembly at mitochondria. We suggest that Srv2 functions as a pro-fission factor in shaping mitochondrial dynamics and regulating activity through its actin-regulatory effects. : Molecular Biology; Cell Biology; Functional Aspects of Cell Biology Subject Areas: Molecular Biology, Cell Biology, Functional Aspects of Cell Biology
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spelling doaj.art-12ea958152794add9e644da674731b1e2022-12-21T18:55:29ZengElsevieriScience2589-00422019-01-0111305317Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin AssemblyYing-Chieh Chen0Tzu-Hao Cheng1Wei-Ling Lin2Chang-Lin Chen3Wei Yuan Yang4Craig Blackstone5Chuang-Rung Chang6Institute of Biotechnology, National Tsing Hua University, Life Science Building II, Room 506 No. 101, Section 2, Kuang-Fu Road, Hsin Chu City 30013, Taiwan, ROCInstitute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei City 11221, Taiwan, ROCInstitute of Biotechnology, National Tsing Hua University, Life Science Building II, Room 506 No. 101, Section 2, Kuang-Fu Road, Hsin Chu City 30013, Taiwan, ROCInstitute of Biotechnology, National Tsing Hua University, Life Science Building II, Room 506 No. 101, Section 2, Kuang-Fu Road, Hsin Chu City 30013, Taiwan, ROCInstitute of Biological Chemistry, Academia Sinica, Taipei City 11529, Taiwan, ROCCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Building 35, Room 2A-201, 9000 Rockville Pike, Bethesda, MD 20892, USA; Corresponding authorInstitute of Biotechnology, National Tsing Hua University, Life Science Building II, Room 506 No. 101, Section 2, Kuang-Fu Road, Hsin Chu City 30013, Taiwan, ROC; Corresponding authorSummary: Dynamic processes such as fusion, fission, and trafficking are important in the regulation of cellular organelles, with an abundant literature focused on mitochondria. Mitochondrial dynamics not only help shape its network within cells but also are involved in the modulation of respiration and integrity. Disruptions of mitochondrial dynamics are associated with neurodegenerative disorders. Although proteins that directly bind mitochondria to promote membrane fusion/fission have been studied intensively, machineries that regulate dynamic mitochondrial processes remain to be explored. We have identified an interaction between the mitochondrial fission GTPase Dnm1/DRP1 and the actin-regulatory protein Srv2/CAP at mitochondria. Deletion of Srv2 causes elongated-hyperfused mitochondria and reduces the reserved respiration capacity in yeast cells. Our results further demonstrate that the irregular network morphology in Δsrv2 cells derives from disrupted actin assembly at mitochondria. We suggest that Srv2 functions as a pro-fission factor in shaping mitochondrial dynamics and regulating activity through its actin-regulatory effects. : Molecular Biology; Cell Biology; Functional Aspects of Cell Biology Subject Areas: Molecular Biology, Cell Biology, Functional Aspects of Cell Biologyhttp://www.sciencedirect.com/science/article/pii/S2589004218302517
spellingShingle Ying-Chieh Chen
Tzu-Hao Cheng
Wei-Ling Lin
Chang-Lin Chen
Wei Yuan Yang
Craig Blackstone
Chuang-Rung Chang
Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
iScience
title Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
title_full Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
title_fullStr Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
title_full_unstemmed Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
title_short Srv2 Is a Pro-fission Factor that Modulates Yeast Mitochondrial Morphology and Respiration by Regulating Actin Assembly
title_sort srv2 is a pro fission factor that modulates yeast mitochondrial morphology and respiration by regulating actin assembly
url http://www.sciencedirect.com/science/article/pii/S2589004218302517
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