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

David G. Winkler | Zendy; I Park | Zendy; T Kim | Zendy; NL Payne | Zendy; C T Walsh | Zendy; Jack L. Strominger | Zendy; Jae Hyuk Shin | Zendy

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

Author(s) -

David G. Winkler,

I Park,

T Kim,

NL Payne,

C T Walsh,

Jack L. Strominger,

Jae Hyuk Shin

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.11.5176

Subject(s) - phosphorylation , cyclin dependent kinase 2 , map2k7 , protein kinase c , kinase , protein kinase a , microbiology and biotechnology , mitogen activated protein kinase kinase , protein phosphorylation , biochemistry , mapk14 , tyrosine kinase , chemistry , biology , signal transduction

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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