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Transformation of rat fibroblasts by phospholipase C‐γ1 overexpression is accompanied by tyrosine dephosphorylation of paxillin
Author(s) -
Chang Jong-Soo,
Iwashita Shintaro,
Lee Young Han,
Kim Myung Jong,
Ryu Sung Ho,
Suh Pann-Ghill
Publication year - 1999
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/s0014-5793(99)01338-1
Subject(s) - paxillin , dephosphorylation , tyrosine phosphorylation , phosphorylation , tyrosine , microbiology and biotechnology , immunoprecipitation , focal adhesion , fibronectin , phospholipase c , chemistry , biology , biochemistry , phosphatase , signal transduction , extracellular matrix , gene
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.