Signal-regulated protein kinases

Protein phosphorylation alters protein ligand binding and/or catalytic functions and hence specific cellular processes, this representing the cellular response to the stimulus of the original primary messenger . The signalling system must be reversible and the protein phosphorylation step of the stimulus-response pathway is reversed through the action of phosphoprotein phosphatases (PPs), which are phosphohydrolases that catalyse the hydrolytic dephosphorylation of proteins  

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PKA and PKC are, however, not the only kinases to regulate TRPVl. The Ca /calmodulin-dependent kinase II (CaMKII) sensitizes TRPVl by phosphorylation [57, 58], as does phophatidylinositol 3-kinase (PI3K) via its downstream target AKT [59]. This latter finding links TRPVl to the ERK (extracellular signal-regulated protein kinase) pathway. The non-receptor tyrosine kinase Src likewise potentiates capsaicin-induced currents [60]. 

Nakayama, H., Numakawa, T., Ikeuchi, T., Hatanaka, H. Nicotine-induced phosphorylation of extracellular signal-regulated protein kinase and CREB in PC12h cells. J. Neurochem. 79 489, 2001. 

The best characterized family of MAPKs in the brain are the extracellular signal-regulated protein kinases (ERKs) that are activated by the neurotrophins and related growth factors (Fig. 23-4) [14,15]. The MAPK kinases responsible... 

MEK mitogen-activated or extracellular signal-regulated protein kinase... 

She QB, Bode AM, Ma WY, Chen NY, Dong Z. 2001. Resveratrol-induced activation of p53 and apoptosis is mediated by extracellular-signal-regulated protein kinases and p38 kinase. Cancer Res 61 1604-1610. 

Siwak DR, Shishodia S, Aggarwal BB, Kurzrock R. 2005. Curcumin-induced antiproliferative and proapoptotic effects in melanoma cells are associated with suppression of IkappaB kinase and nuclear factor kappaB activity and are independent of the B-Raf/mitogen-activated/extracellular signal-regulated protein kinase pathway and the Akt pathway. Cancer 104 879-890. 

Treatment of hippocampal slices with kainate produces a time-dependent increase in NF-/< B levels in areas CA3 and CA1, but not dentate gyrus, compared with controls (Lubin et al., 2005). The kainate-mediated NF-kB complex that binds to DNA is composed of p65, p50, and c-Rel subunits. Pharmacological studies indicate that extracellular signal-regulated protein kinase (ERK) and Ptdlns-3K... 

Lubin F. D., Johnston L. D., Sweatt J. D., and Anderson A. E. (2005). Kainate mediates nuclear factor-kappa B activation in hippocampus via phosphatidylinositol-3 kinase and extracellular signal-regulated protein kinase. Neuroscience 133 969-981. 

Cai G, Zhen X, Uryu K, Friedman E. Activation of extracellular signal regulated protein kinases is associated with a sensitized locomotor response to D(2) dopamine receptor stimulation in unilateral 6-hydroxydopamine lesioned rats. J Neurosci 2000 20 1849-1857. 

Another major linkage of the 5-HT1A receptor is to activation of ERK (extracellular signal regulated protein kinase) in fibroblasts and neuronal cells (43-49). ERK activation by the 5-HT1A receptor is initiated by Py-subunits... 

Gamovskaya MN, Mukhin Y, Raymond JR. Rapid activation of sodium-proton exchange and extracellular signal-regulated protein kinase in fibroblasts by G protein-coupled 5-HT1A receptor involves distinct signalling cascades. Biochem J 1998 330(Pt l) 489-495. 

Another finding is the biphasic phosphorylation of extracellular signal-regulated protein kinase (ERK) during CVB3 entry and replication (Cunningham et al. 2003 ... 

Gliki, G., Abu-Ghazaleh, R., Jezequel, S., Wheeler-Jones, C., and Zachary I. 2001. Vascular endothelial growth factor-induced prostacyclin production is mediated by a protein kinase C (PKC)-dependent activation of extracellular signal-regulated protein kinases 1 and 2 involving PKC-delta and by mobilization of intracellular Ca2+. Biochem. J. 353 503-512. 

Pedram, A., Razandi, M., and Levin, E. R. 1998. Extracellular signal-regulated protein kinase/Jun kinase cross-talk underlies vascular endothelial cell growth factor-induced endothelial cell proliferation. J. Biol. Chem. 273 26722-26728. 

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