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  • NEK10 tyrosine phosphorylates p53 and controls its transcriptional activity.

NEK10 tyrosine phosphorylates p53 and controls its transcriptional activity.

Oncogene (2020-06-21)
Nasir Haider, Previn Dutt, Bert van de Kooij, Jason Ho, Luis Palomero, Miquel Angel Pujana, Michael Yaffe, Vuk Stambolic
ABSTRACT

In response to genotoxic stress, multiple kinase signaling cascades are activated, many of them directed towards the tumor suppressor p53, which coordinates the DNA damage response (DDR). Defects in DDR pathways lead to an accumulation of mutations that can promote tumorigenesis. Emerging evidence implicates multiple members of the NimA-related kinase (NEK) family (NEK1, NEK10, and NEK11) in the DDR. Here, we describe a function for NEK10 in the regulation of p53 transcriptional activity through tyrosine phosphorylation. NEK10 loss increases cellular proliferation by modulating the p53-dependent transcriptional output. NEK10 directly phosphorylates p53 on Y327, revealing NEK10's unexpected substrate specificity. A p53 mutant at this site (Y327F) acts as a hypomorph, causing an attenuated p53-mediated transcriptional response. Consistently, NEK10-deficient cells display heightened sensitivity to DNA-damaging agents. Further, a combinatorial score of NEK10 and TP53-target gene expression is an independent predictor of a favorable outcome in breast cancers.

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Monoclonal ANTI-FLAG® M2 antibody produced in mouse, clone M2, purified immunoglobulin (Purified IgG1 subclass), buffered aqueous solution (10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide)
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Anti-MDM2 (Ab-1) Mouse mAb (IF2), liquid, clone IF2, Calbiochem®
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100 μg
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Triton X-100, laboratory grade
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