FEBS Letters | |
Possible role of protein kinase C in the regulation of intracellular stability of focal adhesion kinase in mouse 3T3 cells | |
Fujimoto, Jiro3  Yaoi, Yoshihito1  Soga, Hisae1  Takenoshita, Seiichi2  Yokota, Jun1  Nagamachi, Yukio2  Yamamoto, Tadashi3  Hatai, Mika1  Mogi, Akira1  | |
[1] Biology Division, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104, Japan;Department of 1st Surgery, Gunma University School of Medicine, 3-39-15 Showa-machi, Maebashi-shi, Gunma 371, Japan;Department of Oncology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan | |
关键词: Calphostin C; Focal adhesion kinase; FAK; Protein kinase C; Fibronectin; Phosphorylation; FAK; pp125125; focal adhesion kinase; 2; 5-MeC; methyl-2; 5-dihydroxycinnamate; PKC; protein kinase C; SDS-PAGE; sodium dodecyl sulfate-polyacrylamide gel electrophoresis; | |
DOI : 10.1016/0014-5793(95)01014-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Effects of various types of protein kinase inhibitor on the adhesion and spreading of BALB/c mouse 3T3 cells and on the phosphorylation and stability of focal adhesion kinase (FAK) in the cells were studied. Inhibitors of protein tyrosine kinases, methyl 2,5-dihydroxycinnamate and herbimycin A, inhibited tyrosine-phosphorylation of FAK and the adhesion of 3T3 cells to fibronectin. Among inhibitors of serine/threonine kinases tested, calphostin C, a specific inhibitor of protein kinase C, inhibited cell spreading rather than cell adhesion, and it induced the decrease of intracellular FAK within 30 min. Inhibitors of tyrosine kinase, A kinase, G kinase, and myosin light chain kinase did not induce such a rapid and specific decrease of FAK. When calphostin C (20 μM) was added to sub-confluent monolayer cultures, serine-phosphorylation of FAK was inhibited by 67% within 2 h, and decrease in the amount of FAK and rounding up of the cells began after 4 h. Label-chase experiments indicated that about 60% of 35S-labeled FAK degraded within 1–2 h after addition of calphostin C to monolayer cultures. These results indicated that serine-phosphorylation of FAK induced by protein kinase C was important in the regulation of metabolic stability of FAK.
【 授权许可】
Unknown
【 预 览 】
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