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Human Herpesvirus-6 Reactivation, Mitochondrial Fragmentation, and the Coordination of Antiviral and Metabolic Phenotypes in ME/CFS - 2020 - Schreiner
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https://www.ncbi.nlm.nih.gov/pubmed/26816379
Science. 2016 Jan 15;351(6270):275-281. doi: 10.1126/science.aab4138.
Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress.
Toyama EQ#1, Herzig S#1, Courchet J2, Lewis TL Jr2, Losón OC3, Hellberg K1, Young NP1, Chen H3, Polleux F2, Chan DC3, Shaw RJ1.
Author information
Abstract
Mitochondria undergo fragmentation in response to electron transport chain (ETC) poisons and mitochondrial DNA-linked disease mutations, yet how these stimuli mechanistically connect to the mitochondrial fission and fusion machinery is poorly understood. We found that the energy-sensing adenosine monophosphate (AMP)-activated protein kinase (AMPK) is genetically required for cells to undergo rapid mitochondrial fragmentation after treatment with ETC inhibitors. Moreover, direct pharmacological activation of AMPK was sufficient to rapidly promote mitochondrial fragmentation even in the absence of mitochondrial stress. A screen for substrates of AMPK identified mitochondrial fission factor (MFF), a mitochondrial outer-membrane receptor for DRP1, the cytoplasmic guanosine triphosphatase that catalyzes mitochondrial fission. Nonphosphorylatable and phosphomimetic alleles of the AMPK sites in MFF revealed that it is a key effector of AMPK-mediated mitochondrial fission.
Copyright © 2016, American Association for the Advancement of Science.
Comment in
26816379
PMCID:
PMC4852862
DOI:
10.1126/science.aab4138
[Indexed for MEDLINE]
Free PMC Article
Human Herpesvirus-6 Reactivation, Mitochondrial Fragmentation, and the Coordination of Antiviral and Metabolic Phenotypes in ME/CFS - 2020 - Schreiner
_______________________
https://www.ncbi.nlm.nih.gov/pubmed/26816379
Science. 2016 Jan 15;351(6270):275-281. doi: 10.1126/science.aab4138.
Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress.
Toyama EQ#1, Herzig S#1, Courchet J2, Lewis TL Jr2, Losón OC3, Hellberg K1, Young NP1, Chen H3, Polleux F2, Chan DC3, Shaw RJ1.
Author information
Abstract
Mitochondria undergo fragmentation in response to electron transport chain (ETC) poisons and mitochondrial DNA-linked disease mutations, yet how these stimuli mechanistically connect to the mitochondrial fission and fusion machinery is poorly understood. We found that the energy-sensing adenosine monophosphate (AMP)-activated protein kinase (AMPK) is genetically required for cells to undergo rapid mitochondrial fragmentation after treatment with ETC inhibitors. Moreover, direct pharmacological activation of AMPK was sufficient to rapidly promote mitochondrial fragmentation even in the absence of mitochondrial stress. A screen for substrates of AMPK identified mitochondrial fission factor (MFF), a mitochondrial outer-membrane receptor for DRP1, the cytoplasmic guanosine triphosphatase that catalyzes mitochondrial fission. Nonphosphorylatable and phosphomimetic alleles of the AMPK sites in MFF revealed that it is a key effector of AMPK-mediated mitochondrial fission.
Copyright © 2016, American Association for the Advancement of Science.
Comment in
- Cell biology: Form follows function for mitochondria. [Nature. 2016]
- AMPK Promotes Autophagy by Facilitating Mitochondrial Fission. [Cell Metab. 2016]
26816379
PMCID:
PMC4852862
DOI:
10.1126/science.aab4138
[Indexed for MEDLINE]
Free PMC Article
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