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Phosphorylation and activation of p40 tyrosine kinase by casein kinase‐1
Author(s) -
Vila Jordi,
Payne D.Michael,
Zioncheck Thomas F.,
Harrison Marietta L.,
Itarte Emilio,
Weber Michael J.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80754-7
Subject(s) - phosphorylation , chemistry , tyrosine kinase , casein kinase 2 , casein kinase 1 , mitogen activated protein kinase kinase , biochemistry , protein kinase a , signal transduction
Because examination of regulatory trans ‐phosphorylations can help elucidate the cellular functions of tyrosyi protein kinases, we have investigated the effects of phosphorylation by casein kinase‐1 on the activity of the p40 tyrosyi protein kinase. We find that casein kinase‐1 can phosphorylate the p40 tyrosyl kinase on serine and threonine residues, in part on a unique tryptic peptide. The phosphorylation induces a substantial increase in the tyrosyl protein kinase activity of p40, in contrast to most instances in which serine/threonine phosphorylation inhibits activity of tyrosyl protein kinases. These findings raise the possibility that p40 might be part of a protein phosphorylation network in which casein kinase‐1 participates.