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. 1993 Jun 1;90(11):5176-80.
doi: 10.1073/pnas.90.11.5176.

Phosphorylation of Ser-42 and Ser-59 in the N-terminal region of the tyrosine kinase p56lck

D G Winkler  1 , I Park, T Kim, N S Payne, C T Walsh, J L Strominger, J Shin
Affiliations

Phosphorylation of Ser-42 and Ser-59 in the N-terminal region of the tyrosine kinase p56lck

D G Winkler et al. Proc Natl Acad Sci U S A. .

Abstract

Ser-42 and Ser-59 in the N-terminal region have been identified as the major phorbol ester-induced phosphorylation sites of p56lck. Phosphorylation of Ser-59 results in a gel shift from 56 kDa to 61 kDa. Simultaneous phosphorylation of Ser-42 and Ser-59 results in a further gel shift to 63 kDa. In vitro kinase assays show that Ser-59 can be uniquely phosphorylated by mitogen-activated protein kinase and that Ser-42 can be phosphorylated by either protein kinase A or protein kinase C.

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