Phosphorylation of Ser-42 and Ser-59 in the N-Terminal Region of the Tyrosine Kinase p56lck

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 v...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-06, Vol.90 (11), p.5176-5180
Main Authors: Winkler, David G., Park, Indal, Kim, TaeUe, Payne, Nicola S., Walsh, Christopher T., Strominger, Jack L., Shin, Jaekyoon
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Antibodies
Biological and medical sciences
Cell Line
Cellulose nitrate
Complementary DNA
Electrophoresis
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Gels
Glutathione Transferase - genetics
Glutathione Transferase - isolation & purification
Glutathione Transferase - metabolism
HeLa Cells
Humans
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Molecular Sequence Data
Molecular Weight
Mutagenesis, Site-Directed
Peptide Mapping
Peptides - chemical synthesis
Peptides - metabolism
Phosphopeptides - metabolism
Phosphorylation
Phosphoserine - metabolism
Protein-Tyrosine Kinases - genetics
Protein-Tyrosine Kinases - isolation & purification
Protein-Tyrosine Kinases - metabolism
Proteins
Recombinant Fusion Proteins - isolation & purification
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Serine
T lymphocytes
Tetradecanoylphorbol Acetate - pharmacology
Threonine
Transferases
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.11.5176