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

FEBS Letters

Mitsui, Ken-ichi¹  Iwashita, Shintaro¹ 

[1] Mitsubishi Kasei Institute of Life Sciences, Machida-shi, Tokyo 194, Japan

关键词: Epidermal growth factor;    Tyrosine phosphorylation;    Phospholipase C;    Cyclic AMP-dependent kinase;    Human carcinoma A431 cell;    EGF;    epidermal growth factor;    PLC-γ;    phospholipase C-γ type;    cAMP;    cyclic AMP;    protein kinase A;    cAMP-dependent protein kinase;    P47;    47 kDa phosphoprotein;    SDS-PAGE;    sodium dodecyi sulfate-polyacrylamide gel electrophoresis;    DMEM;    Dulbecco's modified Eagle's medium;    F12;    Ham's F12 medium;   

DOI  :  10.1016/0014-5793(90)80997-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown