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

Winkler, D G; Park, I; Kim, T; Payne, N S; Walsh, C T; Strominger, J L; Shin, J · Proc Natl Acad Sci U S A · 1993

basic_science · Level V

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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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