Cited by 1,085Mitochondrial Function and PathologyAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

AMP-activated protein kinase mediates mitochondrial fission in response to energy stress

Open access
Toyama, Erin Quan, Herzig, Sébastien, Courchet, Julien, Lewis, Tommy L., Losón, Oliver C., Hellberg, Kristina, Young, Nathan P., Chen, Hsiuchen +3 more·2016·Science

Abstract

How to shape mitochondrial networks: Mitochondria undergo fragmentation or fusion in response to changes in cellular metabolism. Toyama et al. report that adenosine monophosphate-activated protein kinase (AMPK) is both necessary and sufficient to control mitochondrial fragmentation. AMPK functions as a sensor to monitor the energy status of the cell by phosphorylating mitochondrial fission factor (MFF), a protein of the mitochondrial outer membrane. MFF then acts to recruit a cytoplasmic guanosine triphosphatase that promotes mitochondrial fission. Science , this issue p. 275

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  • Under mitochondrial stress, fission is activated by AMPK-mediated phosphorylation of mitochondrial fission factor, facilitating removal of damaged mitochondria.

    “Under mitochondrial stress, fission is activated by AMPK-mediated phosphorylation of mitochondrial fission factor, facilitating the removal of damaged mitochondria43.”

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  1. [21]Duvezin-Caubet S J. Biol. Chem 2006 281 37972 37979 17003040
  2. [37]Mairet-Coello G Neuron 2013 78 94 108 23583109 PMC3784324

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Authors
Toyama, E. Q., Herzig, S., Courchet, J., Lewis, T. L., Losón, O. C., Hellberg, K., Young, N. P., Chen, H., Polleux, F., Chan, D. C., & Shaw, R. J.
Affiliations
  • Salk Institute for Biological Studies (US)
  • Mortimer B. Zuckerman Mind Brain Behavior Institute (US)
  • California Institute of Technology (US)
Corresponding author
  • Toyama, Erin Quan
  • Herzig, Sébastien
  • Shaw, Reuben J.
Venue
Science
Published
2016-01-15
Volume
351
Issue
6270
Pages
275-281
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2269336718
Cited by
1,085
References
41
Citations by year
2026: 87 · 2025: 98 · 2024: 113 · 2023: 93 · 2022: 110 · 2021: 141 · 2020: 120 · 2019: 98 · 2018: 96 · 2017: 82 · 2016: 46
FWCI
55.97
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • CaltechAUTHORS (California Institute of Technology) (submittedVersion)
  • HAL (submittedVersion)
Funders
  • NIH (R01DK080425, R01CA172229, P01 CA120964, R01GM062967, R01GM110039, R01NS089456, K99NS091526)
  • Leona M. and Harry B. Helmsley Charitable Trust (2012-PG-MED002)
  • American Cancer Society (122123-PF-12-029-01-TBE, 123016-PF-PF-12-191-01-TBE)
  • European Molecular Biology Organization (EMBO) (ALTF 1101-2013)
  • George E. Hewitt Foundation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords
AMPK, mitochondrial fission, mitochondrial fragmentation, mitochondrial fusion, energy stress, electron transport chain inhibitors, mitochondrial DNA mutations, mitochondrial fission factor, Drp1, phosphorylation, energy sensing
MeSH terms
Adenosine Monophosphate, Cytoplasm, Dactinomycin, Energy Metabolism, Enzyme Activation, Humans, Microtubule-Associated Proteins, Mitochondria, Molecular Sequence Data, Rotenone, Stress, Physiological, GTP Phosphohydrolases, Amino Acid Motifs, Mitochondrial Proteins, Dynamins, Cell Line, Tumor, AMP-Activated Protein Kinases, Mitochondrial Dynamics

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