Konstantopoulos N, Clark S
University of Melbourne, Department of Medicine, Parkville, Victoria, Australia.
Biochem J. 1996 Mar 1;314 ( Pt 2)(Pt 2):387-90. doi: 10.1042/bj3140387.
Paxillin and focal adhesion kinase (pp125FAK) co-localize in focal adhesions; recently insulin has been shown to stimulate the dephosphorylation of pp125FAK; however, its effect on paxillin is unknown. We show that insulin and IGF-1 can stimulate the dephosphorylation of paxillin in CHOT (overexpress human insulin receptors) and CHO delta CT69 (overexpress insulin receptors lacking C-terminal 69 amino acids) cells. Furthermore, the insulin-receptor C-terminus is not needed for either insulin or IGF-1 to stimulate paxillin or pp125FAK dephosphorylation in the CHO (Chinese-hamster ovary) cell lines used.
桩蛋白和粘着斑激酶(pp125FAK)共定位于粘着斑;最近有研究表明胰岛素可刺激pp125FAK的去磷酸化;然而,其对桩蛋白的影响尚不清楚。我们发现胰岛素和胰岛素样生长因子-1(IGF-1)可刺激CHOT(过表达人胰岛素受体)细胞和CHOδCT69(过表达缺失C末端69个氨基酸的胰岛素受体)细胞中桩蛋白的去磷酸化。此外,在所使用的CHO(中国仓鼠卵巢)细胞系中,胰岛素或IGF-1刺激桩蛋白或pp125FAK去磷酸化并不需要胰岛素受体的C末端。