Involvement of SH2‐SH2‐SH3 domain of phospholipase Cγ1 in NF‐κB signaling

FEBS Letters

Jang, Jong-Soo³  Kim, Jin-Hee¹  Oh, Won-Keun¹  Ryu, Sung-Ho²  Ahn, Jong-Seog¹  Choi, Yong-Kyung¹  Kim, Bo-Yeon¹  Mheen, Tae-Ick¹  Suh, Pann-Ghill²  Kang, Dae-Ook¹ 

[1] Korea Research Institute of Bioscience and Biotechnology, P.O. Box 115, Yusong, Taejon 305-333, South Korea;Department of Life Science, Postech, Pohang, South Korea;Department of Biology, Daejin University, Pochongun, Kyunggido, South Korea

关键词: Nuclear factor κB;    Phospholipase Cγ1;    Protein kinase C;    Mitogen activated protein kinase;    Phosphatidylinositol 3-kinase;    SH2-SH3;   

DOI  :  10.1016/S0014-5793(00)01415-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To directly define the role of phospholipase Cγ1 (PLCγ1) in NF-κB activation, NF-κB promoted luciferase reporter gene plasmid (pNF-κB-Luc) was transfected into rat-3Y1 fibroblasts that overexpress whole PLCγ1 (PLCγ1-3Y1), src homology domains SH2-SH2-SH3 of PLCγ1 (SH223-3Y1) and v-src (Src-3Y1). Transient transfection with pNF-κB-Luc remarkably increased the luciferase activity in all three transformants compared with normal rat-3Y1 cells. Pretreatment with inhibitors of protein tyrosine kinase reduced this increase in luciferase activity, but U73122 (a PLC inhibitor) did not. While PD98059, an inhibitor of mitogen activated protein kinase (MAPK), significantly reduced the luciferase activity, there was no effect by wortmannin and Ro-31-8220, inhibitors of phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC), respectively. This study shows a direct evidence that the SH2-SH2-SH3 region of PLCγ1 contributes to the NF-κB signaling and that MAPK, but not PI3K and PKC, is involved in SH2-SH2-SH3 mediated NF-κB activation in these cells.

【 授权许可】

Unknown