Proteasomes associated with the blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein dnm1

Krisztina Tar; Thomas Dange; Ciyu Yang; Yanhua Yao; Anne Laure Bulteau; Elena Fernandez Salcedo; Stephen Braigen; Frederic Bouillaud; Daniel Finley; Marion Schmidt

doi:10.1074/jbc.M114.554105

Proteasomes associated with the blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein dnm1

Krisztina Tar, Thomas Dange, Ciyu Yang, Yanhua Yao, Anne Laure Bulteau, Elena Fernandez Salcedo, Stephen Braigen, Frederic Bouillaud, Daniel Finley, Marion Schmidt

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

Background: Blm10 binds to the proteasome core particle and stimulates its proteolytic activity. Results: Loss of BLM10 results in impaired respiration, elevated oxidative stress sensitivity, increased mitochondrial fission, and stabilization of the fission protein Dnm1. Conclusion: Blm10 proteasome-mediated Dnm1 degradation is a regulatory mechanism to maintain correct mitochondrial function. Significance: Blm10 is involved in mitochondrial quality control under oxidative stress.

Original language	English (US)
Pages (from-to)	12145-12156
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	289
Issue number	17
DOIs	https://doi.org/10.1074/jbc.M114.554105
State	Published - Apr 25 2014
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Proteasomes associated with the blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein dnm1",

abstract = "Background: Blm10 binds to the proteasome core particle and stimulates its proteolytic activity. Results: Loss of BLM10 results in impaired respiration, elevated oxidative stress sensitivity, increased mitochondrial fission, and stabilization of the fission protein Dnm1. Conclusion: Blm10 proteasome-mediated Dnm1 degradation is a regulatory mechanism to maintain correct mitochondrial function. Significance: Blm10 is involved in mitochondrial quality control under oxidative stress.",

author = "Krisztina Tar and Thomas Dange and Ciyu Yang and Yanhua Yao and Bulteau, {Anne Laure} and Salcedo, {Elena Fernandez} and Stephen Braigen and Frederic Bouillaud and Daniel Finley and Marion Schmidt",

year = "2014",

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doi = "10.1074/jbc.M114.554105",

language = "English (US)",

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T1 - Proteasomes associated with the blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein dnm1

AU - Tar, Krisztina

AU - Dange, Thomas

AU - Yang, Ciyu

AU - Yao, Yanhua

AU - Bulteau, Anne Laure

AU - Salcedo, Elena Fernandez

AU - Braigen, Stephen

AU - Bouillaud, Frederic

AU - Finley, Daniel

AU - Schmidt, Marion

PY - 2014/4/25

Y1 - 2014/4/25

N2 - Background: Blm10 binds to the proteasome core particle and stimulates its proteolytic activity. Results: Loss of BLM10 results in impaired respiration, elevated oxidative stress sensitivity, increased mitochondrial fission, and stabilization of the fission protein Dnm1. Conclusion: Blm10 proteasome-mediated Dnm1 degradation is a regulatory mechanism to maintain correct mitochondrial function. Significance: Blm10 is involved in mitochondrial quality control under oxidative stress.

AB - Background: Blm10 binds to the proteasome core particle and stimulates its proteolytic activity. Results: Loss of BLM10 results in impaired respiration, elevated oxidative stress sensitivity, increased mitochondrial fission, and stabilization of the fission protein Dnm1. Conclusion: Blm10 proteasome-mediated Dnm1 degradation is a regulatory mechanism to maintain correct mitochondrial function. Significance: Blm10 is involved in mitochondrial quality control under oxidative stress.

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JO - Journal of Biological Chemistry

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IS - 17

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Proteasomes associated with the blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein dnm1

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