Abstract
p21-activated kinase (PAK) targeting to the plasma membrane is essential for PC12 cell neurite outgrowth. Phospholipase C-γ1 (PLC-γ1) can mediate the PAK translocation in response to growth factors, since PLC-γ1 binds to both tyrosine-phosphorylated receptor tyrosine kinases and PAK through its SH2 and SH3 domain, respectively. In the present study, we examined a potential role for PLC-γ1 in the basic fibroblast growth factor (bFGF)-induced PAK translocation using stable PC12 cell lines that overexpress in a tetracycline-inducible manner either the wild-type FGFR-1 or the Y766F FGFR-1 mutant. Phosphatidylinositol hydrolysis was increased 6.5-fold in response to bFGF in the wild type cells but negligible in the mutant cells. The recombinant GST-PLC-γ1 SH3 was able to bind to PAK1 but not GST alone. However, examination of PLC-γ1 as an adaptor for translocation of PAK1 in cells showed that both cells transfected with pEGFP-PAK1 was able to differentiate for 24 h, as visualized by laser confocal microscopy. Translocation of PAK1 to growth cones occurs at similar levels in both wild and mutant cells. These results suggest that a protein(s) other than PLC-γ1 is functionally relevant for PAK targeting.
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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Shin, KS., Shin, EY., Lee, CS. et al. Basic fibroblast growth factor-induced translocation of p21-activated kinase to the membrane is independent of phospholipase C-γ1 in the differentiation of PC12 cells. Exp Mol Med 34, 172–176 (2002). https://doi.org/10.1038/emm.2002.25
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DOI: https://doi.org/10.1038/emm.2002.25