The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis
Open accessAbstract
Phosphorylation is often used to promote protein ubiquitylation, yet we rarely understand quantitatively how ligase activation and ubiquitin (UB) chain assembly are integrated with phospho-regulation. Here we employ quantitative proteomics and live-cell imaging to dissect individual steps in the PINK1 kinase-PARKIN UB ligase mitochondrial control pathway disrupted in Parkinson’s Disease. PINK1 plays a dual role by phosphorylating PARKIN on its UB-like domain and poly-UB chains on mitochondria. PARKIN activation by PINK1 produces canonical and non-canonical UB chains on mitochondria, and PARKIN-dependent chain assembly is required for accumulation of poly-phospho-UB (poly-p-UB) on mitochondria. In vitro, PINK1 directly activates PARKIN’s ability to assemble canonical and non-canonical UB chains, and promotes association of PARKIN with both p-UB and poly-p-UB. Our data reveal a feed-forward mechanism that explains how PINK1 phosphorylation of both PARKIN and poly-UB chains synthesized by PARKIN drives a program of PARKIN recruitment and mitochondrial ubiquitylation in response to mitochondrial damage.
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Citations
Cites
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
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PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
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PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
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Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
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Self-citationUbiquitin is phosphorylated by PINK1 to activate parkin
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Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
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PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
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Self-citationLandscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
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Self-citationBroad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
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Cited by
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Self-citationMechanism and medical implications of mammalian autophagy
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The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,081
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
Metadata
- Authors
- Ordureau, A., Sarraf, S. A., Duda, D. M., Heo, J.-M., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., Wells, J. A., Gygi, S. P., Schulman, B. A., & Harper, J. W.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2014-11
- Volume
- 56
- Issue
- 3
- Pages
- 360-375
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1996625702
- Cited by
- 697
- References
- 42
- FWCI
- 32.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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- The paper
- Ordureau, A., Sarraf, S. A., Duda, D. M., Heo, J.-M., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., Wells, J. A., Gygi, S. P., Schulman, B. A., & Harper, J. W. (2014). Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis. Molecular Cell. https://doi.org/10.1016/j.molcel.2014.09.007
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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