STIMULATION OF TYROSINE-PHOSPHORYLATION AND SERINE-PHOSPHORYLATION OF FOCAL ADHESION KINASE IN MOUSE 3T3 CELLS BY FIBRONECTIN AND FIBROBLAST GROWTH-FACTOR

被引：41

作者：

HATAI, M ^{[1
]}

HASHI, H ^{[1
]}

MOGI, A ^{[1
]}

SOGA, H ^{[1
]}

YOKOTA, J ^{[1
]}

YAOI, Y ^{[1
]}

机构：

[1] TAKARA SHUZO CO, BIOTECHNOL RES LABS, SHIGA 52021, JAPAN

来源：

FEBS LETTERS | 1994年 / 350卷 / 01期

关键词：

FOCAL ADHESION KINASE; FIBRONECTIN; FIBROBLAST GROWTH FACTOR; PHOSPHORYLATION;

D O I：

10.1016/0014-5793(94)00745-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphorylation of both tyrosine and serine residues of focal adhesion kinase (FAK) was stimulated by the adhesion of BALB/c mouse 3T3 cells to fibronectin, but phosphorylation of threonine was not detectable. Acidic and basic fibroblast growth factors also stimulated the phosphorylation of serine and tyrosine of FAK in cells adhered to poly-L-lysine, but epidermal growth factor and platelet-derived growth factor did not. A fusion protein of fibronectin and basic fibroblast growth factor effectively induced the phosphorylation of FAK. Phosphorylation of FAK in the rat myoblast L-6 cell line, which lacks fibroblast growth factor receptors, was not stimulated by fibroblast growth factors, suggesting that the interaction of fibroblast growth factors with their receptors might cause the phosphorylation of FAK.

引用

页码：113 / 116

页数：4

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