QBI - Seminar

QBI Seminar: Conserved roles for Cysteine residues in (pseudo)kinases

The QBI Seminar Series is presenting Pat Eyers, Professor of Cell Signaling in the Department of Biochemistry at the University of Liverpool. He and his multidisciplinary research lab study the roles of Cys residues in eukaryotic protein kinases. His seminar will focus on recent findings that demonstrate the catalytic activity of the Ser/Thr kinase Aurora A is inhibited by oxidation of a conserved cysteine residue in the regulatory activation segment.

Analysis revealed that ~100 human Ser/Thr kinases also possess a Cys at the equivalent position, which is prognostic for redox-sensitivity amongst a cohort of human CAMK, AGC and AGC-like kinases, including PKA, AKT, AMPK, CAMK1, MAPKAP-K2/3, MELK, SIK1-3 and PLK1/4. Dr. Eyers and his lab predict that redox modulation of Cys residue equivalents in Ser/Thr kinases may be an underappreciated regulatory mechanism that is widespread in eukaryotes. Given the key biological roles of these enzymes, their work has significant implications both for understanding physiological and pathological responses to ROS and for covalent drug targeting in kinases. Finally, they highlight the importance of protein kinase regulation through multivalent modification of the activation segment.

Dr. Eyers obtained an undergraduate degree in Biochemistry at the University of Bristol, and completed his PhD with Sir Philip Cohen at the University of Dundee. After 4 years of postdoctoral research in the USA with Jim Maller, he set up his laboratory in the UK with an MRC Career Development Fellowship in 2005. His interests include all aspects of protein phosphorylation and sulfation, analysis of protein kinase and sulfotransferase regulation, pseudokinases and pseudoenzymes and understanding kinome-wide mechanisms of acquired drug-resistance in cells.

Talk title: Conserved roles for Cysteine residues in (pseudo)kinases

Hosted by: Natalia Jura

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