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02/02/2012 09:24 | After taking a month break next week I have to back to work. I've had a little travel with my family in the past month, and believe it or not, I never thought i could be so happy.
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Cells recognize and respond to extracellular stimuli by engaging specific intracellular programs, such as the signaling cascade that leads to activation of the mitogen-activated protein kinases (MAPKs). All eukaryotic cells possess multiple MAPK pathways, which coordinately regulate diverse cellular activities running the gamut from gene expression, mitosis, and metabolism to motility, survival and apoptosis, and differentiation. To date, five distinct groups of MAPKs have been characterized in mammals: extracellular signal-regulated kinases (ERKs) 1 and 2 (ERK1/2), c-Jun amino-terminal kinases (JNKs) 1, 2, and 3, p38 isoforms ¦Á, ¦Â, ¦Ã, and¦Ä , ERKs 3 and 4, and ERK5 (reviewed in references 25 and 103). Since Saccharomyces cerevisiae possesses six different MAPKs, the relative complexity of the human genome suggests that there are probably several additional vertebrate MAPK subfamilies (118). The most extensively studied groups of vertebrate MAPKs to date are the ERK1/2, JNKs, and p38 kinases.
MAPKs can be activated by a wide variety of different stimuli, but in general, ERK1 and ERK2 are preferentially activated in response to growth factors and phorbol esters, while the JNK and p38 kinases are more responsive to stress stimuli ranging from osmotic shock and ionizing radiation to cytokine stimulation (reviewed in reference 147) (Fig. 1). Although each MAPK has unique characteristics, a number of features are shared by the MAPK pathways studied to date. Each family of MAPKs is composed of a set of three evolutionarily conserved, sequentially acting kinases: a MAPK, a MAPK kinase (MAPKK), and a MAPKK kinase (MAPKKK). The MAPKKKs, which are serine/threonine kinases, are often activated through phosphorylation and/or as a result of their interaction with a small GTP-binding protein of the Ras/Rho family in response to extracellular stimuli (36, 98). MAPKKK activation leads to the phosphorylation and activation of a MAPKK, which then stimulates MAPK activity through dual phosphorylation on threonine and tyrosine residues located in the activation loop of kinase subdomain VIII. Once activated, MAPKs phosphorylate target substrates on serine or threonine residues followed by a proline; however, substrate selectivity is often conferred by specific interaction motifs located on physiological substrates. Furthermore, MAPK cascade specificity is also mediated through interaction with scaffolding proteins which organize pathways in specific modules through simultaneous binding of several components. |
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