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Nature Reviews Drug Discovery 19, 579 (2020)
doi: https://doi.org/10.1038/d41573-020-00116-x
Acknowledgements
This article is part of a series from the NIH Common Fund Illuminating the Druggable Genome (IDG) program. The goal of IDG is to catalyse research on understudied proteins from druggable gene families by providing reagents, phenotypes and a mineable database; focusing on GPCRs, kinases and ion channels. For more information, see https://druggablegenome.net/
Updates & Corrections
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Update 21 July 2020: Further studies on STK19 have been reported very recently that are important to note in the context of this article, which discusses results from a 2019 paper by Yin et al. (Cell 176, 1113–1127; 2019). Rodríguez-Martínez et al. published a paper (Cell 181, 1295–1405; 2020) raising questions about the conclusions of the 2019 paper by Yin et al., including the annotation of STK19, the physiological relevance of a 41 kDa isoform of STK19 studied by Yin et al., whether STK19 is a canonical kinase and whether the D98N mutation is a melanoma driver. Yin et al. provided a response (Cell 181, 1406–1049; 2020), including follow-up experiments to confirm their original findings. Support for these original findings has also come from independent research by Qian et al. discussed in this article, which showed that STK19 is a kinase that binds ATP with NRAS as a substrate (Clin. Cancer Res. 26, 3408–3419; 2020). This was investigated with the aid of a narrow-spectrum kinase inhibitor, chelidonine, that was shown to directly inhibit STK19, as was the case with the compound ZT-12-037-01 reported by Yin et al. (Cell 176, 1113–1127; 2019). For both compounds, NRAS was used as substrate, and testing of direct ATP binding/phosphorylation as well as recording of DSF melt curves was performed, all of which support the rationale that STK19 is a kinase.
Competing Interests
The authors declare no competing interests.
