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A computational resource can identify candidate protein targets for almost all members of a major class of kinase enzyme in humans, with implications for understanding cell signalling in health and disease.
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- Sean J. Humphrey0 &
- Elise J. Needham1
- Sean J. Humphrey
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Sean J. Humphrey is at the Murdoch Children’s Research Institute, Royal Children’s Hospital, Melbourne, Victoria 3052, Australia.
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- Elise J. Needham
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Elise J. Needham is in the BHF Cardiovascular Epidemiology Unit, Department of Public Health and Primary Care, University of Cambridge, Cambridge CB2 0BA, UK.
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Protein phosphorylation — the selective addition of phosphate groups to proteins — is a regulatory mechanism that is fundamental to life. Conversely, dysregulated phosphorylation has been implicated in conditions such as Alzheimer’s disease, cancer and diabetes1. The enzymes that catalyse phosphorylation, known as kinases, are major targets for drugs2, so understanding their regulatory roles could provide new therapeutic opportunities. Advances in our ability to identify and quantify phosphorylation using mass spectrometry has led to a rapid rise in the number of known phosphorylation sites in human proteins (collectively known as the phosphoproteome), from hundreds at the turn of the century to more than 100,000 today3. However, linking these sites with their associated kinases has been a laborious process3. Writing in Nature, Johnson et al.4 take a major step towards resolving this problem, describing a comprehensive resource that defines the potential substrates for almost all members of one major class of human kinase.
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Nature 613, 637-638 (2023)
doi: https://doi.org/10.1038/d41586-022-04583-7
References
Cohen, P. Nature Rev. Drug Discov. 1, 309–315 (2002).
Attwood, M. M., Fabbro, D., Sokolov, A. V., Knapp, S. & Schiöth, H. B. Nature Rev. Drug Discov. 20, 839–861 (2021).
Needham, E. J., Parker, B. L., Burykin, T., James, D. E. & Humphrey, S. J. Sci. Signal. 12, eaau8645 (2019).
Johnson, J. L. et al. Nature 613, 759–766 (2023).
Humphrey, S. J., James, D. E. & Mann, M. Trends Endocrinol. Metab. 26, 676–687 (2015).
Hutti, J. E. et al. Nature Methods 1, 27–29 (2004).
Sharma, K. et al. Cell Rep. 8, 1583–1594 (2014).
Zhu, G. et al. J. Biol. Chem. 280, 10743–10748 (2005).
Manning, G., Whyte, D. B., Martinez, R., Hunter, T. & Sudarsanam, S. Science 298, 1912–1934 (2002).
Jumper, J. et al. Nature 596, 583–589 (2021).
Edwards, A. M. et al. Nature 470, 163–165 (2011).
Aebersold, R. & Mann, M. Nature 537, 347–355 (2016).
Obenauer, J. C., Cantley, L. C. & Yaffe, M. B. Nucleic Acids Res. 31, 3635–3641 (2003).
Linding, R. et al. Nucl. Acids Res. 36, D695–D699 (2008).
Ochoa, D. et al. Nature Biotechnol. 38, 365–373 (2020).
Competing Interests
The authors declare no competing interests.
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