A Common Phosphate Binding Site Explains the Unique Substrate Specificity of GSK3 and Its Inactivation by Phosphorylation

The inhibition of GSK3 is required for the stimulation of glycogen and protein synthesis by insulin and the specification of cell fate during development. Here, we demonstrate that the insulin-induced inhibition of GSK3 and its unique substrate specificity are explained by the existence of a phospha...

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Veröffentlicht in:	Molecular cell 2001-06, Vol.7 (6), p.1321-1327
Hauptverfasser:	Frame, Sheelagh, Cohen, Philip, Biondi, Ricardo M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arginine - metabolism Axin Protein b-catenin beta Catenin Binding Sites - physiology Calcium-Calmodulin-Dependent Protein Kinases - chemistry Calcium-Calmodulin-Dependent Protein Kinases - genetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell Line Cytoskeletal Proteins - metabolism Diabetes Mellitus, Type 2 - metabolism glycogen synthase Glycogen Synthase Kinase 3 Humans Leucine - genetics Molecular Sequence Data Mutagenesis, Site-Directed Phosphates - metabolism Phosphorylation Protein Structure, Tertiary Proteins - metabolism Repressor Proteins Serine - metabolism Substrate Specificity Trans-Activators Wnt protein
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