Amino acid sequence at the site on protein phosphatase inhibitor-2, phosphorylated by glycogen synthase kinase-3

• Published in: Biochimica et biophysica acta Vol. 790; no. 3; pp. 288 - 291
• Main Authors: Aitken, Alastair, Holmes, Charles F.B., Campbell, David G., Resink, Therese J., Cohen, Philip, Leung, Christine T.W., Williams, Dudley H.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.01.1984; Elsevier; North-Holland
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Calcium-Calmodulin-Dependent Protein Kinases; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Glycogen synthase kinase; Glycogen Synthase Kinases; Hydrolases; Inhibitor-2; phosphoprotein phosphatase; Phosphoprotein Phosphatases - antagonists & inhibitors; Phosphorylated residue; Phosphorylation; Primary structure; protein kinase; Protein Kinases - metabolism; Protein phosphatase; Proteins - metabolism; Primary structure; Protein phosphatase; Inhibitor-2; Glycogen synthase kinase; Phosphorylated residue; Proteins; Reversed phase chromatography; Phosphorylation; Radiolabelling; Enzyme; Phosphoprotein phosphatase; Catalyst activity; Mass spectrometry
• ISSN: 0167-4838; 0006-3002; 1879-2588; 1878-2434
• DOI: 10.1016/0167-4838(84)90034-7

The primary structure surrounding the residue on Inhibitor-2 phosphorylated by glycogen synthase kinase-2 has been determined. The sequence is: Lys-Ile-Asp-Glu-Pro-Ser-Thr(P)-Pro-Tyr-His-Ser. This finding will facilitate studies of the effects of hormones on the phosphorylation state of Inhibitor-2 in vitvo.