Research ArticleBiochemistry

Engineering allosteric regulation in protein kinases

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Science Signaling  06 Nov 2018:
Vol. 11, Issue 555, eaar3250
DOI: 10.1126/scisignal.aar3250

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Hotspots of kinase regulation

The addition of phosphate moieties can alter protein conformation, function, abundance, and localization, thereby regulating a myriad of cellular behaviors and responses. These sites are often mutated in cancer and other diseases. Pincus et al. mapped the residue alignment and patterning of phosphoregulatory sites in eukaryotic kinases and determined that kinases share a conserved architecture, such that introducing a target motif of the kinase PKA at surface sites within two different yeast kinases altered their activity, pathway interactions, and subcellular localization, as well as the overall response of the yeast to pheromone and osmotic signals, in a PKA-dependent manner. These findings, which reveal insights into kinase evolution, also have implications for biological engineering and medicine.