Regulation of translation elongation factor‐2 by insulin via a rapamycin‐sensitive signalling pathway.

摘要: It is well established that insulin and serum stimulate gene expression at the level of mRNA translation in animal cells, previous studies have mainly focused on initiation process. Here we show that, Chinese hamster ovary cells expressing human receptor, causes decreased phosphorylation elongation factor eEF-2 this associated with stimulation rate peptide-chain elongation. phosphorylated by a very specific Ca 2+/calmodulin-dependent protein kinase (eEF-2 kinase) causing its complete inactivation. The decrease induced reflects fall activity. Rapamycin, macrolide immunosuppressant which blocks signalling pathway leading to 70/85 kDa ribosomal S6 kinases, substantially activation elongation, activity, suggesting p7O (p70s6k) may tie common pathway. Wortmannin, an inhibitor phosphatidylinositide-3-OH kinase, had similar effects. was vitro purified p70s6k but no significant effect activity kinase.