Protein kinase recognition sequence motifs

作者: Bruce E. Kemp , Richard B. Pearson

DOI: 10.1016/0968-0004(90)90073-K

关键词:

摘要: Protein kinases play a crucial role in the regulation of many cellular processes. They alter functions their target proteins by phosphorylating specific serine, threonine and tyrosine residues. Identification phosphorylation site sequences studies with corresponding model peptides have provided clues to how these important enzymes recognize substrate proteins. This knowledge has made it possible identify potential sites newly sequenced as well construct substrates inhibitors.

参考文章(26)
S S Taylor, cAMP-dependent protein kinase. Model for an enzyme family. Journal of Biological Chemistry. ,vol. 264, pp. 8443- 8446 ,(1989) , 10.1016/S0021-9258(18)81805-1
Thomas A. Langan, Isolation of histone kinases. Methods in Cell Biology. ,vol. 19, pp. 143- 152 ,(1978) , 10.1016/S0091-679X(08)60019-9
W P Hausdorff, M Bouvier, B F O'Dowd, G P Irons, M G Caron, R J Lefkowitz, Phosphorylation sites on two domains of the β2-adrenergic receptor are involved in distinct pathways of receptor desensitization Journal of Biological Chemistry. ,vol. 264, pp. 12657- 12665 ,(1989) , 10.1016/S0021-9258(18)63907-9
W Rychlik, M A Russ, R E Rhoads, Phosphorylation site of eukaryotic initiation factor 4E. Journal of Biological Chemistry. ,vol. 262, pp. 10434- 10437 ,(1987) , 10.1016/S0021-9258(18)60978-0
P R Vulliet, F L Hall, J P Mitchell, D G Hardie, Identification of a novel proline-directed serine/threonine protein kinase in rat pheochromocytoma. Journal of Biological Chemistry. ,vol. 264, pp. 16292- 16298 ,(1989) , 10.1016/S0021-9258(18)71620-7
J L Countaway, I C Northwood, R J Davis, Mechanism of phosphorylation of the epidermal growth factor receptor at threonine 669. Journal of Biological Chemistry. ,vol. 264, pp. 10828- 10835 ,(1989) , 10.1016/S0021-9258(18)81695-7
R B Pearson, J R Woodgett, P Cohen, B E Kemp, Substrate specificity of a multifunctional calmodulin-dependent protein kinase. Journal of Biological Chemistry. ,vol. 260, pp. 14471- 14476 ,(1985) , 10.1016/S0021-9258(17)38593-9