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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2002.1
- 수록면
- 12 - 176 (165page)
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p21-activated kinase (PAK) targeting to the plasmamembrane is essential for PC12 cell neurite out-growth. Phospholipase C- g1 (PLC-g1) can mediatethe PAK translocation in response to growth factors,since PLC-g1 binds to both tyrosine-phosphorylatedreceptor tyrosine kinases and PAK through its SH2and SH3 domain, respectively. In the present study,we examined a potential role for PLC- g1 in the basicfibroblast growth factor (bFGF)-induced PAK trans-location using stable PC12 cell lines that over-expres in a tetracycline-inducible manner either thewild-type FGFR-1 or the Y766F FGFR-1 mutant.Phosphatidylinositol hydrolysis was increased 6.5-fold in response to bFGF in the wild type cels butnegligible in the mutant cells. The recombinant GST-PLC-g1 SH3 was able to bind to PAK1 but not GSTalone. However, examination of PLC- g1 as an adap-tor for translocation of PAK1 in cells showed thatboth cells transfected with pEGFP-PAK1 was able todifferentiate for 24 h, as visualized by laser confocalmicroscopy. Translocation of PAK1 to growth conesoccurs at similar levels in both wild and mutant cells.These results suggest that a protein(s) other thanPLC-g1 is functionally relevant for PAK targeting.
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