TAILIEUCHUNG - Báo cáo sinh học: "Dimerization in protein kinase signaling"

Tuyển tập các báo cáo nghiên cứu về sinh học được đăng trên tạp chí sinh học Journal of Biology đề tài: Dimerization in protein kinase signaling. | J. Biol. Journal of Biology BioMed Central Comment Dimerization in protein kinase signaling Steven Pelech Address The Brain Research Centre Division of Neurology 2211 Wesbrook Mall University of British Columbia Vancouver BC V6T 2B5 Canada. Email spelech@ Published 19 July 2006 Journal of Biology 2006 5 12 The electronic version of this article is the complete one and can be found online at http content 5 5 12 2006 BioMed Central Ltd Abstract The closely related mitogen-activated protein kinases ERK1 and ERK2 have now been shown to have opposing roles in Ras-mediated cell proliferation. I propose that dimerization of these highly related protein kinases could underlie these surprising observations and that this could be a common paradigm for widespread regulation of protein phosphorylation by kinase-substrate interactions. Two closely related mitogen-activated protein MAP kinases extracellular signal-regulated protein kinase ERK 1 and ERK2 are known to be involved in the regulation of cell proliferation. These ubiquitous protein-serine threonine kinases are well known as key players in signaling pathways downstream of growth-factor receptor-tyrosine kinases cytokine receptors and G-protein-coupled receptors 1 they often indirectly mediate the actions of members of the Ras family of small GTPases. Gain-of-function mutations have been implicated in more than 30 of human tumors but chronic activation of Ras by mutated mitogen receptors occurs in even higher frequency than this 2 . Most previously published work has inferred that ERK1 and ERK2 are commonly regulated and that they target the same substrates. In this issue of the Journal of Biology however Riccardo Brambilla and colleagues 3 provide compelling evidence that the two ERK proteins in fact counteract each other in the regulation of the cell-proliferation effects of Ras in mouse fibroblasts. Vantaggiato and Formentini et al. 3 have demonstrated that induced reduction of ERK1 expression .

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