ArticlePloS one2019
Parkin-mediated ubiquitination contributes to the constitutive turnover of mitochondrial fission factor (Mff).
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- The Mitochondrial Foundations of Parkinson's Disease: Therapeutic Implications.Aging and disease · 2025Review
- SUMOylation of MFF coordinates fission complexes to promote stress-induced mitochondrial fragmentation.Science advances · 2024Article
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- TRAF3: A novel regulator of mitochondrial physiology and metabolic pathways in B lymphocytes.Frontiers in oncology · 2023Review
- Mitochondrial fusion- and fission-related protein expression in the regulation of skeletal muscle mass.Physiological reports · 2022Article
- Multitasking guardian of mitochondrial quality: Parkin function and Parkinson's disease.Translational neurodegeneration · 2021Review
- Mitochondrial Fission Factor Is a Novel Interacting Protein of the Critical B Cell Survival Regulator TRAF3 in B Lymphocytes.Frontiers in immunology · 2021Article
- Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function.Neuronal signaling · 2020Review
- Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The mitochondrial outer membrane protein Mitochondrial Fission Factor (Mff) plays a key role in both physiological and pathological fission. It is well established that at stressed or functionally impaired mitochondria, PINK1 recruits the ubiquitin ligase Parkin which ubiquitinates Mff and other mitochondrial outer membrane proteins to facilitate the removal of defective mitochondria and maintain the integrity of the mitochondrial network. Here we show that, in addition to this clearance pathway, Parkin also ubiquitinates Mff in a PINK1-dependent manner under non-stressed conditions to regulate constitutive Mff turnover. We further show that removing Parkin via shRNA-mediated knockdown does not completely prevent Mff ubiquitination under these conditions, indicating that at least one other ubiquitin ligase contributes to Mff proteostasis. These data suggest that that Parkin plays a role in physiological maintenance of mitochondrial membrane protein composition in unstressed cells through constitutive low-level activation.
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Registered trials
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