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Possible role of protein kinase C in the regulation of intracellular stability of focal adhesion kinase in mouse 3T3 cells
Author(s) -
Mogi Akira,
Hatai Mika,
Soga Hisae,
Takenoshita Seiichi,
Nagamachi Yukio,
Fujimoto Jiro,
Yamamoto Tadashi,
Yokota Jun,
Yaoi Yoshihito
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01014-6
Subject(s) - focal adhesion , intracellular , microbiology and biotechnology , chemistry , kinase , protein kinase a , ptk2 , ask1 , mitogen activated protein kinase kinase , phosphorylation , biology
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 35 S‐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.