A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
Open accessAbstract
Mitochondria have long been implicated in the pathogenesis of Parkinson's disease (PD). Mutations in the mitochondrial kinase PINK1 that reduce kinase activity are associated with mitochondrial defects and result in an autosomal-recessive form of early-onset PD. Therapeutic approaches for enhancing the activity of PINK1 have not been considered because no allosteric regulatory sites for PINK1 are known. Here, we show that an alternative strategy, a neo-substrate approach involving the ATP analog kinetin triphosphate (KTP), can be used to increase the activity of both PD-related mutant PINK1(G309D) and PINK1(WT). Moreover, we show that application of the KTP precursor kinetin to cells results in biologically significant increases in PINK1 activity, manifest as higher levels of Parkin recruitment to depolarized mitochondria, reduced mitochondrial motility in axons, and lower levels of apoptosis. Discovery of neo-substrates for kinases could provide a heretofore-unappreciated modality for regulating kinase activity.
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Simultaneous treatment with kinetin triphosphate (KTP) did not enhance T0466 or T0467 efficacy.
“Simultaneous treatment with a previously characterized PINK1 activation molecule, kinetin triphosphate (KTP), did not enhance T0466 or T0467 efficacy (Figure S2A) (Hertz et al., 2013).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Hertz et al., 2013
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Structure of human PINK1 at a mitochondrial TOM-VDAC array
Callegari, S., Kirk, N. S., Gan, Z. Y., Dite, T., Cobbold, S. A., Leis, A., Dagley, L. F., Glukhova, A., & Komander, D. (2025) · Science · doi:10.1126/science.adu6445 · Cited by 75 · see citing works
A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling
Shiba-Fukushima, K., Inoshita, T., Sano, O., Iwata, H., Ishikawa, K.-I., Okano, H., Akamatsu, W., Imai, Y., & Hattori, N. (2020) · iScience · doi:10.1016/j.isci.2020.101048 · Cited by 37 · see citing works
- Authors
- Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M.
- Affiliations
- Howard Hughes Medical Institute (US)
- Gladstone Institutes (US)
- University of California, San Francisco (US)
- Corresponding author
- Shokat, Kevan M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-08
- Volume
- 154
- Issue
- 4
- Pages
- 737-747
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3950538
- OpenAlex
- W2044235925
- Cited by
- 275
- References
- 81
- Citations by year
- 2026: 19 · 2025: 13 · 2024: 16 · 2023: 18 · 2022: 26 · 2021: 31 · 2020: 25 · 2019: 25 · 2018: 23 · 2017: 28 · 2016: 18 · 2015: 13 · 2014: 12 · 2013: 7
- FWCI
- 10.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Wellcome Trust
- National Institutes of Health (5r01eb001987-15)
- National Institute of General Medical Sciences (P41GM103481)
- National Institute of Neurological Disorders and Stroke (P30NS069496, 1KO8NS062954-01A1, K08NS062954)
- National Institute of Biomedical Imaging and Bioengineering (R01-EB001987)
- National Center for Research Resources (RR015804, RR 001614, P41RR001614, S10RR015804)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- PINK1, Parkinson's disease, kinase activation, mitochondrial depolarization, mitochondrial motility, axons, apoptosis, allosteric regulation, mitochondrial dysfunction
- MeSH terms
- PTEN-Induced Putative Kinase, Adenosine Triphosphate, Amino Acid Sequence, Animals, Axons, Cell Line, Cells, Cultured, Hippocampus, Humans, Kinetin, Mice, Inbred C57BL, Mitochondria, Molecular Sequence Data, Neurons, Parkinson Disease, Phosphorylation, Protein Kinases, Sequence Alignment, Apoptosis, Ubiquitin-Protein Ligases, bcl-X Protein, Mice, Rats
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