Kim S H, Yang Y C
Hansol Biotechnology and Protein Function Research Unit, Korea Research Institute of Bioscience & Biotechnology, KIST, South Korea.
Biochem Biophys Res Commun. 1996 Dec 13;229(2):577-81. doi: 10.1006/bbrc.1996.1846.
The possible formation of a stable complex between extracellular signal-regulated kinases (ERKs) and Raf protein kinases was investigated in an attempt to understand the molecular mechanism by which Raf protein kinases were differentially regulated in response to the various stimuli, leading to the activation of ERKs in rat hippocampus. ERK3 was found to coelute with B-Raf, but not c-Raf1, after fractionation of rat hippocampal lysates by QMA anionic exchange chromatography. ERK3 was released into soluble supernatant fraction from the B-Raf, but not c-Raf1, immunoprecipitate, after incubation with ATP. These results, taken together, suggest the specific association of ERK3 with B-Raf in rat hippocampus.
为了理解Raf蛋白激酶在各种刺激下如何被差异调节从而导致大鼠海马体中细胞外信号调节激酶（ERK）激活的分子机制，研究了细胞外信号调节激酶（ERK）与Raf蛋白激酶之间可能形成的稳定复合物。在用QMA阴离子交换色谱法分离大鼠海马体裂解物后，发现ERK3与B-Raf共洗脱，但不与c-Raf1共洗脱。与ATP孵育后，ERK3从B-Raf免疫沉淀复合物中释放到可溶性上清液组分中，而不是从c-Raf1免疫沉淀复合物中释放。综合这些结果，表明在大鼠海马体中ERK3与B-Raf存在特异性结合。
