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Dissection of novel protein kinase cascades that are triggered by insulin


The main aim of this project is to elucidate the molecular mechanism by which insulin regulates the synthesis of glycogen and other biosynthetic processes in mammalian skeletal muscle.
It is well known that defects in the regulation of glycogen synthase (GS) by insulin contribute to the insulin resistence observed in NIDDM patiens, obesity, hypertension and IDDM. The activation of GS by insulin is achieved through the inhibition of GS Kinase 3 (GSK3). Recents evidences showed that this inhibition is caused in vivo by its phosphorylation by the protein kinase c-Akt. In its turn, c-Akt is activated by phosphorylation in response to insulin. Recent experiments in the MRC Protein phosphorylation Unit have identified a novel insulin-stimulated protein kinase which phosphorylates a synthetic peptide corresponding to one region of the c-Akt protein.
The objective of the project is to characterise the protein kinase(s) and phosphatase(s) responsible for the catalysis of the
phospho-dephosphorilation of c-Akt and to discover how it is activated by insulin. The elucidation of this important insulin signal transduction pathway may contribute to the development of treatments of diabetes.


University of Dundee
DD1 4HN Dundee
United Kingdom

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