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Examination of the role of serine phosphorylation in phospholipase C‐γ and its related P47 in cAMP‐mediated depression of epidermal growth factor receptor signal transduction
Author(s) -
Mitsui Ken-ichi,
Iwashita Shintaro
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)80997-w
Subject(s) - phosphorylation , epidermal growth factor , forskolin , serine , phospholipase c , signal transduction , protein phosphorylation , biology , protein kinase c , kinase , phosphoserine , protein kinase a , biochemistry , receptor , microbiology and biotechnology , chemistry
Forskolin‐pretreatment ofA431 cells reduced both intrinsic and epidermal growth factor (EGF)‐induced EGF receptor phosphorylation, however, phosphorylation of pospholipase c‐γ (PLC‐γ) was stimulated under the same conditions. No significant difference was detected in the amount of phosphotyrosine of PLC‐γ between two cultures with or without forskolin treatment followed by EGF. On the other hand, phosphorylation of a 47 kDa protein (P47) which cross‐reacted with an anti‐PLC‐y monoclonal antibody, was stimulated by both forskolin and EGF. Phosphorylation was exclusively on serine residues in this case. These results indicate that both PLC‐γ and P47 are posphorylated by a cAMP‐dependent protein kinase and the EGF‐stimulated serine kinase, and suggest that serine phosphorylation of PLC‐γ has no effect on ligand‐dependent coupling with the EGF receptor.