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Protein Chemistry
Laboratory / Group Name: Protein Chemistry & Metabolism
Group Leader: Prof Bruce E. Kemp
Project Leaders:
Postdoc:
Overview
The protein chemistry & metabolism laboratory is interested in how protein phosphorylation regulates protein function. Protein kinases and protein phosphatases catalyse the attachment and removal of phosphate groups from proteins and are involved in the control of most physiological processes. Intracellular protein function is controlled by protein phosphorylation, often at multiple sites and involving multiple protein kinases and phosphatases. Previously our work has identified how protein kinases recognize their substrates and how a number of protein kinases are regulated. Our current efforts are focussed on the metabolic stress enzyme, AMP-activated protein kinase (AMPK) that is responsible for controlling metabolism in response to energy demand (exercise) and energy availability (food intake). It is well recognized that diet and exercise influence health and longevity and our group is concerned with how AMPK matches metabolism to nutrient supply and energy demand for many physiological processes. We are interested in the detailed structure, function and regulation of AMPK as well as its downstream signaling targets. This work may provide important opportunities for drug design and particularly in understanding how exercise protects the body from the development of age onset diseases that include obesity, diabetes, hypertension, stroke, neurodegeneration and cardiovascular disease.
