INTERLEUKIN-1 ACTIVATES A NOVEL PROTEIN-KINASE CASCADE THAT RESULTS IN THE PHOSPHORYLATION OF HSP27
INTERLEUKIN-1 ACTIVATES A NOVEL PROTEIN-KINASE CASCADE THAT RESULTS IN THE PHOSPHORYLATION OF HSP27
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DOI：
10.1016/0092-8674(94)90278-x
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发表时间：
1994-09-23
期刊：
影响因子：
64.5
通讯作者：
SAKLATVALA, J
中科院分区：
文献类型：
--
作者：
FRESHNEY, NW;RAWLINSON, L;SAKLATVALA, J
已经在KB细胞中鉴定了IL-1刺激的蛋白激酶级联，其导致小的热休克蛋白hsp 27的磷酸化。它与p42 MAP激酶级联反应不同。上游激活激酶磷酸化苏氨酸和酪氨酸残基上的40 kDa激酶（p40），其进而磷酸化苏氨酸（和一些丝氨酸）残基上的50 kDa激酶（p50）。p50在丝氨酸作用下磷酸化HSP 27。将p40和p50纯化至接近同质。所有这三种成分都被蛋白磷酸酶2A灭活，而p40被蛋白酪氨酸磷酸酶1B灭活。p40的底物特异性不同于p42和p54 MAP激酶。上游激活剂不是MAP激酶激酶。p50与MAPKAPK-2相似，可能是相同的。
An IL-1-stimulated protein kinase cascade resulting in phosphorylation of the small heat shock protein hsp27 has been identified in KB cells. It is distinct from the p42 MAP kinase cascade. An upstream activator kinase phosphorylated a 40 kDa kinase (p40) upon threonine and tyrosine residues, which in turn phosphorylated a 50 kDa kinase (p50) upon threonine (and some serine) residues. p50 phosphorylated hsp27 upon serine. p40 and p50 were purified to near homogeneity. All three components were inactivated by protein phosphatase 2A, and p40 was inactivated by protein tyrosine phosphatase 1B. The substrate specificity of p40 differed from that of p42 and p54 MAP kinases. The upstream activator was not a MAP kinase kinase. p50 resembled MAPKAPK-2 and may be identical.