Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase
Open accessAbstract
Mutations in Parkin represent ~50% of disease-causing defects in autosomal recessive-juvenile onset Parkinson's disease (AR-JP). Recently, there have been four structural reports of autoinhibited forms of this RING-IBR-RING (RBR) ubiquitin ligase (E3) by the Gehring, Komander, Johnston and Shaw groups. The important advances from these studies set the stage for the next steps in understanding the molecular basis for Parkinson's disease (PD).
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Proteasomal 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 [34]
The Abstract says activating Parkin mutations may lead to increased autoubiquitination and degradation. It separately says Parkin promotes proteasomal degradation of mitochondrial proteins and mitophagy. It does not demonstrate that Parkin itself is proteasomally degraded during mitophagy or that this halts its activity. (LLM, conf=0.86)
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Research works printed but not linked: 2
- Hardy J, Lewis P, Revesz T, Lees A, Paisan-Ruiz C (2009) The genetics of Parkinson's syndromes: a critical review. Curr Opin Genet Dev 19: 254-265
- Metzger MB, Pruneda JN, Klevit RE, Weissman AM (2013) RING- type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim Biophys Acta pii:S0167- 4889(13)00216-4. doi:10.1016/j.bbamcr.2013.05.026 · DOI
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Altered mitochondrial dynamics and function in APOE4-expressing astrocytes
Schmukler, E., Solomon, S., Simonovitch, S., Goldshmit, Y., Wolfson, E., Michaelson, D. M., & Pinkas-Kramarski, R. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-02776-4 · Cited by 125 · see citing works
Moussa, C. E.-H. (2015) · Neurodegenerative Diseases · doi:10.1159/000430888 · Cited by 13 · see citing works
- Authors
- Byrd, R. A., & Weissman, A. M.
- Affiliations
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Byrd, R Andrew
- Weissman, Allan M
- Venue
- The EMBO Journal
- Published
- 2013-07-12
- Volume
- 32
- Issue
- 15
- Pages
- 2087-2089
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3730235
- OpenAlex
- W2093242149
- Cited by
- 23
- References
- 0
- Citations by year
- 2026: 1 · 2021: 1 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 5 · 2014: 4
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Parkin, RBR E3 ubiquitin ligase, autoinhibition, Parkinson's disease, protein structure, protein degradation regulation
- MeSH terms
- Animals, Humans, Mutation, Structure-Activity Relationship, Protein Structure, Tertiary, Parkinsonian Disorders, Ubiquitin-Protein Ligases
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