Extracellular Regulated Kinase Phosphorylates Mitofusin 1 to Control Mitochondrial Morphology and Apoptosis
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Controlled changes in mitochondrial morphology participate in cellular signaling cascades. However, the molecular mechanisms modifying mitochondrial shape are largely unknown. Here we show that the mitogen-activated protein (MAP) kinase cascade member extracellular-signal-regulated kinase (ERK) phosphorylates the pro-fusion protein mitofusin (MFN) 1, modulating its participation in apoptosis and mitochondrial fusion. Phosphoproteomic and biochemical analyses revealed that MFN1 is phosphorylated at an atypical ERK site in its heptad repeat (HR) 1 domain. This site proved essential to mediate MFN1-dependent mitochondrial elongation and apoptosis regulation by the MEK/ERK cascade. A mutant mimicking constitutive MFN1 phosphorylation was less efficient in oligomerizing and mitochondria tethering but bound more avidly to the proapoptotic BCL-2 family member BAK, facilitating its activation and cell death. Moreover, neuronal apoptosis following oxygen glucose deprivation and MEK/ERK activation required an intact MFN1(T562). Our data identify MFN1 as an ERK target to modulate mitochondrial shape and apoptosis.
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Mitochondrial size and shape as well as lipid composition can influence the likelihood of mitochondria to undergo irreversible MOMP.
“Finally, it is becoming increasingly evident that mitochondrial size and shape [139–141] as well as lipid composition [142, 143] can influence the likelihood of mitochondria to undergo irreversible MOMP.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [139]
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- Authors
- Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L.
- Affiliations
- University of Padua (IT)
- Friedrich Miescher Institute (CH)
- Corresponding author
- Scorrano, Luca
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 58
- Issue
- 2
- Pages
- 244-254
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4405354
- OpenAlex
- W2041542870
- Cited by
- 244
- References
- 53
- Citations by year
- 2026: 16 · 2025: 25 · 2024: 24 · 2023: 21 · 2022: 15 · 2021: 27 · 2020: 27 · 2019: 21 · 2018: 22 · 2017: 25 · 2016: 17 · 2015: 4
- FWCI
- 9.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Molecular Cell (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitofusin 1, ERK1/2 phosphorylation, mitochondrial morphology, mitochondrial fusion, apoptosis, MEK/ERK signaling, Bak, mitochondrial elongation, neuronal apoptosis, oxygen-glucose deprivation, phosphoproteomics
- MeSH terms
- Animals, Cells, Cultured, Fibroblasts, Membrane Proteins, Mitochondria, Neurons, Phosphorylation, Rats, Wistar, Apoptosis, Oxidative Stress, GTP Phosphohydrolases, MAP Kinase Signaling System, Mitochondrial Proteins, Proteomics, Mice, Rats, Mitochondrial Dynamics
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