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Tyrosine phosphorylation and stimulation of protein kinase Cδ from porcine spleen by src in vitro
Author(s) -
Gschwendt Michael,
Kielbassa Kirsten,
Kittstein Walter,
Marks Friedrich
Publication year - 1994
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(94)00514-1
Subject(s) - phosphorylation , proto oncogene tyrosine protein kinase src , protein kinase c , tyrosine phosphorylation , protein tyrosine phosphatase , tyrosine kinase , tyrosine , activator (genetics) , tyrosine protein kinase csk , fyn , chemistry , microbiology and biotechnology , protein phosphorylation , biology , biochemistry , sh2 domain , protein kinase a , signal transduction , receptor
Native protein kinase Cδ from porcine spleen is phosphorylated in vitro by the tyrosine kinase src and to a much smaller extent by fyn. The tyrosine phosphorylation of PKCδ is restricted to the activated state of the enzyme, i.e. it occurs only in the presence of an activator, such as TPA or bryostatin. Upon phosphorylation at tyrosine, the apparent molecular weight of PKCδ increases by 6 kDa. Phosphorylation by src induces a stimulation of PKCδ activity apparently exhibiting some substrate selectivity. Other PKC isoenzymes, such as cPKC (α,β,γ), are not phosphorylated by src or only to a very small extent. This phosphorylation is not dependent on TPA and does not cause an increase in activity and molecular weight of the enzyme.