Parkin structure and function
Open accessAbstract
Mutations in the parkin or PINK 1 genes are the leading cause of the autosomal recessive form of Parkinson's disease. The gene products, the E3 ubiquitin ligase parkin and the serine/threonine kinase PINK 1, are neuroprotective proteins, which act together in a mitochondrial quality control pathway. Here, we review the structure of parkin and mechanisms of its autoinhibition and function as a ubiquitin ligase. We present a model for the recruitment and activation of parkin as a key regulatory step in the clearance of depolarized or damaged mitochondria by autophagy (mitophagy). We conclude with a brief overview of other functions of parkin and considerations for drug discovery in the mitochondrial quality control pathway.
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Both PINK1 and Parkin have neuroprotective roles against various insults, such as oxidative stress and PD-relevant toxins.
“Beyond their roles in mitophagy, mounting evidence suggested that both PINK1 and Parkin have neuroprotective roles against various insults, such as oxidative stress and PD-relevant toxins, although the underlying mechanisms still remain elusive [22, 23].”
From miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1) (2016) · cites this paper as [22]
The Abstract calls both PINK1 and parkin neuroprotective, and “Other functions of parkin” says they work together to repair mitochondria in response to mild oxidative stress. The References include studies of parkin protecting neurons against toxins, but the paper does not establish comparable protection by PINK1 against PD-relevant toxins. (LLM, conf=0.82)
Experimental — accuracy not yet measuredProteasomal degradation of parkin occurs during mitophagy due to autoubiquitination, halting its activity.
“Proteasomal degradation of parkin was demonstrated during mitophagy due to autoubiquitination, halting its activity28,29,33,34.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [28]
The section ‘Parkin is an RBR E3 ubiquitin ligase’ (page unavailable) says parkin becomes ubiquitinated and that this may play a role in its own degradation during the mitophagy pathway. It does not establish that parkin is degraded by the proteasome, that autoubiquitination causes that degradation, or that degradation halts its activity. (LLM, conf=0.88)
Experimental — accuracy not yet measuredParkin labels mitochondria for mitophagy by ubiquitinating specific mitochondrial proteins; parkin is then degraded by the proteasome/lysosome due to autoubiquitination.
“Parkin labels mitochondria for mitophagy by ubiquitinating specific mitochondrial proteins; parkin is then degraded by the proteasome/lysosome due to autoubiquitination26–29.”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [28]
The Introduction and “Parkin is an RBR E3 ubiquitin ligase” section say that parkin ubiquitinates outer mitochondrial membrane proteins, marking damaged mitochondria for mitophagy. The latter section says K6 ubiquitination of parkin may play a role in its own degradation; it does not establish that parkin is subsequently degraded by the proteasome or lysosome because of autoubiquitination. (LLM, conf=0.90)
Experimental — accuracy not yet measuredAPOE4 astrocytes exhibit increased parkin levels.
“increased parkin levels (targets mitochondria for mitophagy, followed by proteasomal/lysosomal degradation26–29)”
From Altered mitochondrial dynamics and function in APOE4-expressing astrocytes (2020) · cites this paper as [28]
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Short Mitochondrial ARF Triggers Parkin/PINK1-dependent Mitophagy
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The genetics of Parkinson disease
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“Beyond their roles in mitophagy, mounting evidence suggested that both PINK1 and Parkin have neuroprotective roles against various insults, such as oxidative stress and PDrelevant toxins, although the underlying mechanisms still remain elusive [22, 23].”
BackgroundCysteines as Redox Molecular Switches and Targets of Disease
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Molecular changes in the postmortem parkinsonian brain
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Interaction between Parkin and α-Synuclein in PARK2-Mediated Parkinson’s Disease
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The Role of Mitophagy in Regulating Cell Death
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Loss of Microglial Parkin Inhibits Necroptosis and Contributes to Neuroinflammation
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Parkinson's Disease Modification Through Abl Kinase Inhibition: An Opportunity
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Gp78 E3 Ubiquitin Ligase: Essential Functions and Contributions in Proteostasis
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Deficit in PINK1/PARKIN-mediated mitochondrial autophagy at late stages of dystrophic cardiomyopathy
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Parkinson's disease‐associated protein Parkin: an unusual player in cancer
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Lipids, lysosomes and mitochondria: insights into Lewy body formation from rare monogenic disorders
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Post translational modification of Parkin
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Parkin regulates NF-κB by mediating site-specific ubiquitination of RIPK1
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A mutational atlas for Parkin proteostasis
Clausen, L., Voutsinos, V., Cagiada, M., Johansson, K. E., Grønbæk-Thygesen, M., Nariya, S., Powell, R. L., Have, M. K. N., Oestergaard, V. H., Stein, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45829-4 · Cited by 51 · see citing works
The synaptic function of parkin
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Hypoxia Signaling in Parkinson’s Disease: There Is Use in Asking “What HIF?”
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Structural basis for feedforward control in the PINK1/Parkin pathway
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Parkin regulates lipopolysaccharide-induced proinflammatory responses in acute lung injury
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N-Acetyl-Cysteine: Modulating the Cysteine Redox Proteome in Neurodegenerative Diseases
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Discovery of small-molecule positive allosteric modulators of Parkin E3 ligase
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HIV-1 Tat and Cocaine Impair Survival of Cultured Primary Neuronal Cells via a Mitochondrial Pathway
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Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of HSC70-Interacting Protein
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Parkin and mitochondrial signalling
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The role of E3 ubiquitin ligases in synapse function in the healthy and diseased brain
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Chapter Five - Ubiquitination of Ion Channels and Transporters
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Structure of the second phosphoubiquitin–binding site in parkin
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Self-citationParkin: a potential target to promote healthy ageing
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Imaging Findings and Toxicological Mechanisms of Nervous System Injury Caused by Diquat
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Deubiquitinating Enzymes in Parkinson’s Disease
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Regulation of Parkin expression as the key balance between neural survival and cancer cell death
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Quantitative Middle-Down MS Analysis of Parkin-Mediated Ubiquitin Chain Assembly
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A PINK1 input threshold arises from positive feedback in the PINK1/Parkin mitophagy decision circuit
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Saikia, B. J., Bhardwaj, J., Paul, S. C., Sharma, S., Neog, A., Paul, S. R., & Binukumar, B. K. (2023) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2023.111838 · Cited by 19 · see citing works
Zhong, Y., Li, X., Du, X., Bi, M., Ma, F., Xie, J., & Jiang, H. F. (2020) · Scientific Reports · doi:10.1038/s41598-020-72630-2 · Cited by 21 · see citing works
Danışman, B., Kelek, S. E., & Aslan, M. (2023) · Psychiatry and Clinical Psychopharmacology · doi:10.5152/pcp.2023.23633 · Cited by 19 · see citing works
Genetic Variations and Neuropathologic Features of Patients with PRKN Mutations
Seike, N., Yokoseki, A., Takeuchi, R., Saito, K., Miyahara, H., Miyashita, A., Ikeda, T., Aida, I., Nakajima, T., Kanazawa, M., et al. (2021) · Movement Disorders · doi:10.1002/mds.28521 · Cited by 19 · see citing works
Mitochondrial autophagy in the sleeping brain
Mauri, S., Favaro, M., Bernardo, G., Mazzotta, G. M., & Ziviani, E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.956394 · Cited by 20 · see citing works
Zhang, W., Hou, W., Chen, M., Chen, E., Xue, D., Ye, C., Li, W., & Pan, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576104 · Cited by 19 · see citing works
Prkn knockout mice show autistic-like behaviors and aberrant synapse formation
Huo, Y., Lü, W., Tian, Y., Hou, Q., & Man, H. (2022) · iScience · doi:10.1016/j.isci.2022.104573 · Cited by 19 · see citing works
Recent Advances in the Treatment of Genetic Forms of Parkinson’s Disease: Hype or Hope?
Cavallieri, F., Cury, R. G., Guimarães, T. G., Fioravanti, V., Grisanti, S., Rossi, J., Monfrini, E., Zedde, M., Fonzo, A. D., Valzania, F., et al. (2023) · Cells · doi:10.3390/cells12050764 · Cited by 18 · see citing works
- Authors
- Seirafi, M., Kozlov, G., & Gehring, K.
- Affiliations
- McGill University (CA)
- Corresponding author
- Gehring, Kalle
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2015-03-16
- Volume
- 282
- Issue
- 11
- Pages
- 2076-2088
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- PMC
- PMC4672691
- OpenAlex
- W2013828402
- Cited by
- 256
- References
- 86
- Citations by year
- 2026: 19 · 2025: 24 · 2024: 29 · 2023: 37 · 2022: 27 · 2021: 38 · 2020: 26 · 2019: 16 · 2018: 11 · 2017: 17 · 2016: 9 · 2015: 3
- FWCI
- 1.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- FEBS Journal (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (MOP-125924)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Parkin, PINK1, Parkinson's disease, mitochondrial quality control, mitophagy, E3 ubiquitin ligase, autoinhibition, protein structure, mitochondrial depolarization, neuroprotection, drug discovery
- MeSH terms
- Amino Acid Sequence, Animals, Humans, Mitochondria, Molecular Sequence Data, Neurons, Parkinson Disease, Protein Transport, Ubiquitin-Protein Ligases, Ubiquitination, Mitophagy
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