An investigation will be made of the properties and regulation of glycogen synthase in rabbit muscle and liver in vitro and in vivo. Synthase kinases will be purified and characterized from muscle and liver. Regulation of kinases by calcium, calmodulin, and cyclic nucleotides will be examined. Relationships between phosphorylation, activity, and structure of synthase will be studied. Binding of glucose-6-P and UDP-glucose to muscle synthase will be determined. Phosphorylation of synthase in vivo will be studied in response to epinephrine, insulin, and diabetes. Effects of somatostatin infusion will be examined. The in vivo phosphorylation state of each of the sites in muscle synthase will be determined by analysis of tryptic peptides separated by high performance liquid chromatography.
Perrino, B A; Ng, L Y; Soderling, T R (1995) Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain. J Biol Chem 270:340-6 |
Filipek, A; Soderling, T R (1993) Identification of an autoinhibitory domain in the insulin receptor tyrosine kinase. Mol Cell Biochem 120:103-10 |
Shibata, H; Robinson, F W; Soderling, T R et al. (1991) Effects of okadaic acid on insulin-sensitive cAMP phosphodiesterase in rat adipocytes. Evidence that insulin may stimulate the enzyme by phosphorylation. J Biol Chem 266:17948-53 |
Brickey, D A; Colbran, R J; Fong, Y L et al. (1990) Expression and characterization of the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II using the baculovirus expression system. Biochem Biophys Res Commun 173:578-84 |
Yang, S D; Chang, S Y; Soderling, T R (1987) Characterization of an autophosphorylation-dependent multifunctional protein kinase from liver. J Biol Chem 262:9421-7 |