Pink1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy
Open accessAbstract
Mitochondrial fission is essential for the degradation of damaged mitochondria. It is currently unknown how the dynamin-related protein 1 (DRP1)-associated fission machinery is selectively targeted to segregate damaged mitochondria. We show that PTEN-induced putative kinase (PINK1) serves as a pro-fission signal, independently of Parkin. Normally, the scaffold protein AKAP1 recruits protein kinase A (PKA) to the outer mitochondrial membrane to phospho-inhibit DRP1. We reveal that after damage, PINK1 triggers PKA displacement from A-kinase anchoring protein 1. By ejecting PKA, PINK1 ensures the requisite fission of damaged mitochondria for organelle degradation. We propose that PINK1 functions as a master mitophagy regulator by activating Parkin and DRP1 in response to damage. We confirm that PINK1 mutations causing Parkinson disease interfere with the orchestration of selective fission and mitophagy by PINK1.
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PINK1 can serve as a pro-fission signal by activating DRP1 in response to mitochondrial damage.
“PINK1 can serve as a pro-fission signal by activating DRP1 in response to mitochondria damage (96).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [96]
Exercise-induced Pink1 activation of Drp1 could target dysfunctional mitochondria for mitophagy.
“Exercise-induced Pink1 activation of Drp1 (112) could also target dysfunctional mitochondria for mitophagy.”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [112]
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References 35 · Cited by 185
- Authors
- Pryde, K. R., Smith, H. L., Chau, K.-Y., & Schapira, A. H. V.
- Affiliations
- UCL Queen Square Institute of Neurology (GB)
- University College London (GB)
- Corresponding author
- Pryde, Kenneth R.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2016-04-18
- Volume
- 213
- Issue
- 2
- Pages
- 163-171
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC5084273
- OpenAlex
- W2337123977
- Cited by
- 185
- References
- 35
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 15 · 2023: 20 · 2022: 23 · 2021: 32 · 2020: 20 · 2019: 13 · 2018: 15 · 2017: 21 · 2016: 5
- FWCI
- 16.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust
- Medical Research Council (WT089698)
- National Institute of Health Research (RCF30AS2012, RCF73TS20145989, RCF103/AS/2014)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- PINK1, mitophagy, mitochondrial fission, Drp1, AKAP1, protein kinase A, Parkin, mitochondrial damage, Parkinson's disease, mitochondrial outer membrane
- MeSH terms
- PTEN-Induced Putative Kinase, Calcium, Cell Line, Humans, Mitochondria, Phosphorylation, Protein Kinases, Substrate Specificity, Gene Silencing, Ubiquitin-Protein Ligases, Mitochondrial Dynamics, Mitophagy
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