Transformation of rat fibroblasts by phospholipase C‐γ1 overexpression is accompanied by tyrosine dephosphorylation of paxillin

FEBS Letters

Kim, Myung Jong⁴  Ryu, Sung Ho⁴  Suh, Pann-Ghill⁴  Iwashita, Shintaro³  Chang, Jong-Soo¹  Lee, Young Han² 

[1] Department of Biology, Daejin University, Pochon-gun, Kyeonggido 487-800, South Korea;Department of Biochemistry, College of Medicine, Yeungnam University, Taegu 705-717, South Korea;Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida-shi, Tokyo 194, Japan;Department of Life Science, Pohang University of Science and Technology, POSTECH, Pohang 790-784, South Korea

关键词: Phospholipase C-γ1;    Paxillin;    Cell adhesion;    Phosphorylation;   

DOI  :  10.1016/S0014-5793(99)01338-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously have shown that the overexpression of phospholipase C-γ1 (PLC-γ1) in rat 3Y1 fibroblasts results in malignant transformation (Chang, J.-S., Noh, D.Y., Park, I.A., Kim, M.J., Song, H., Ryu, S.H. and Suh, P.-G. (1997) Cancer Res. 57, 5465–5468). The transformed cells, which initially are in an elongated and flat form after seeding in plastic dishes, become rounded during continued culture. We found that tyrosine dephosphorylation of paxillin accompanies this morphological change of the transformed cells and that PLC-γ1 co-immunoprecipitates together with paxillin and vice versa, but not after the cells have become round. Transformed cells growing on fibronectin-pre-coated dishes regain their flat morphology and this is accompanied by paxillin tyrosine phosphorylation. Furthermore, immunoprecipitation analysis showed that paxillin forms a heteromeric complex with PLC-γ1 in cells grown on fibronectin. These results suggest that a complex formation between paxillin and PLC-γ1 may play a role in cell-substrate adhesion.

【 授权许可】

Unknown