Mertens S, Craxton M, Goedert M
MRC Laboratory of Molecular Biology, Cambridge, UK.
FEBS Lett. 1996 Apr 1;383(3):273-6. doi: 10.1016/0014-5793(96)00255-4.
Stress-activated protein kinases are MAP kinase homologues that are activated by cellular stresses, bacterial endotoxin and inflammatory cytokines. They are activated by a dual threonine/tyrosine phosphorylation within a TPY sequence in the case of stress-activated protein kinase-1 and its isoforms (also called JNKs) or a TGY sequence in the case of stress-activated protein kinase-2 and its isoforms (also called p38, p40, RK, CSBPs, XMpk2 and Mxi2). Here we report the cloning and sequencing of a new protein kinase from rat with a TGY sequence in the activation domain. This stress-activated protein kinase-3 is 60% identical to mouse stress-activated protein kinase-2 and 45% identical to HOG1 from Saccharomyces cerevisiae. Transcripts encoding stress-activated protein kinase-3 are widely expressed, with high levels in skeletal muscle.
应激激活蛋白激酶是丝裂原活化蛋白激酶(MAP激酶)的同源物,可被细胞应激、细菌内毒素和炎性细胞因子激活。对于应激激活蛋白激酶-1及其同工型(也称为JNKs),它们通过TPY序列内的双苏氨酸/酪氨酸磷酸化而被激活;对于应激激活蛋白激酶-2及其同工型(也称为p38、p40、RK、CSBPs、XMpk2和Mxi2),则通过TGY序列被激活。在此,我们报道了从大鼠中克隆和测序的一种新的蛋白激酶,其激活结构域中有一个TGY序列。这种应激激活蛋白激酶-3与小鼠应激激活蛋白激酶-2有60%的同源性,与酿酒酵母的HOG1有45%的同源性。编码应激激活蛋白激酶-3的转录本广泛表达,在骨骼肌中表达水平较高。