Enzymology of protein kinases and phosphatases involved in cancer and neurodegeneration (Signal Transduction, Enzymology, Parkinson's disease, Cancer, Protein Kinases, Phosphatases)
Parkinson's disease (Biochemistry and cell signaling)
Heung-Chin Cheng has been studying the biochemical basis of regulation of protein kinases and phosphatases since he was a graduate student in Dr Donal Walsh's laboratory in the University of California, Davis in 1982. His PhD project unravelled the active site structure of cAMP-dependent protein kinase, how the kinase recognises its protein substrates and how the kinase is selectively inhibited by its endogenous inhibitor. His work contributed to the determination of the crystal structure of the catalytic sub-unit of the kinase. In 1987, he joined Dr. Choh Hao Li's laboratory in the University of California at San Francisco as a postdoctoral fellow and work on a project to characterise the beta-endorphin receptor. After Dr. Li's untimely death, he joined Dr. Jerry Wang's laboratory as MRC postdoctoral fellow. When he was in Dr Jerry Wang's laboratory in the University of Calgary, he extended his interest into protein tyrosine kinases and phosphatases. He defined the substrate selectivity determinants of the Src-family kinases.
After he joined the University of Melbourne, Heung-Chin continued to study how Src-family kinases are regulated by their endogenous inhibitors CSK and CHK. His group identified two new auto phosphorylation sites in the kinases and discovered for the first time that CHK employed a unique non-catalytic mechanism to inhibit Src-family kinase activity. An Associate Professor with the Department of Biochemistry and Molecular Biology, Heung-Chin relocated his research group to the Bio21 Institute in 2005. Since then, his group has been studying the enzymology of two protein kinases, PINK1 and LRRK2, involved in the pathogenesis of Parkinson's disease. In addition to protein kinases, his group is active in studying the catalytic and regulatory properties of the tumour suppressor phosphatase PTEN.