Calcium/calmodulin-dependent protein kinases activation

Shackelford, D. A., and Zivin, J. A. (1993) Renaturation of calcium/calmodulin-dependent protein kinase activity after electrophoretic transfer from sodium dodecyl sulfate-poly-acrylamide gels to membranes. Anal. Biochem. 211, 131-138. 

Akiyama, K., Suemaru, J. Effect of acute and chronic administration of methamphetamine on calcium-calmodulin dependent protein kinase II activity in the rat brain. Ann. N.Y. Acad. Sci. 914 263, 2000. 

FIGURE 1 2-2 Schematic diagram of the phosphorylation sites on each of the four 60kDa subunits of tyrosine hydroxylase (TOHase). Serine residues at the N-terminus of each of the four subunits of TOHase can be phosphorylated by at least five protein kinases. (J), Calcium/calmodulin-dependent protein kinase II (CaM KII) phosphorylates serine residue 19 and to a lesser extent serine 40. (2), cAMP-dependent protein kinase (PKA) phosphorylates serine residue 40. (3), Calcium/phosphatidylserine-activated protein kinase (PKC) phosphorylates serine 40. (4), Extracellular receptor-activated protein kinase (ERK) phosphorylates serine 31. (5), A cdc-like protein kinase phosphorylates serine 8. Phosphorylation on either serine 19 or 40 increases the activity of TOHase. Serine 19 phosphorylation requires the presence of an activator protein , also known as 14-3-3 protein, for the expression of increased activity. Phosphorylation of serines 8 and 31 has little effect on catalytic activity. The model shown includes the activation of ERK by an ERK kinase. The ERK kinase is activated by phosphorylation by PKC. (With permission from reference [72].)... 

Protein kinase Cd, Akt kinase, calcium/calmodulin-dependent protein kinase IV, mitogen-activated protein kinase kinase (MEKK-1), focal adhesion kinase (FAK), protein phosphatase (PP)2A, calcineurin... 

Communi, D. Dewaste, V. Erneux, C. Calcium-calmodulin-dependent protein kinase II and protein kinase C-mediated phosphorylation and activation of D-myo-inositol 1,4, 5-trisphosphate 3-kinase B in astrocytes. J. Biol. Chem., 274, 14734-14742 (1999)... 

Enslen H., Tokumitsu H., Stork R J., Davis R. J., and Soderling T. R. (1996). Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade. Proc. Natl. Acad. Sci. USA 93 10803-10808. 

Moriguchi S., Han F., Nakagawasai O., Tadano T., and Fukunaga K. (2006). Decreased calcium/calmodulin-dependent protein kinase II and protein kinase C activities mediate impairment of hippocampal long-term potentiation in the olfactory bulbectomized mice. J. Neurochem. 97 22-29. 

Chow, F. A., Anderson, K. A., Noeldner, P. K. and Means, A. R., 2005, The autonomous activity of calcium/calmodulin-dependent protein kinase IV is required for its role in transcription, J Biol Chem, 280, pp 20530-8. 

Haribabu, B., Hook, S. S., Seibert, M. A., Goldstein, E. G., Tomhave, E. D., Edelman, A. M., Snyderman, R. and Means, A. R., 1995, Human calcium-calmodulin dependent protein kinase I cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase, Embo J, 14, pp 3679—3686. 

Calcium/calmodulin-dependent protein kinase II (CaM kinase II) is a mediator of synaptic and cytoskeletal function as well as neurotransmitter release. The reduced CaM kinase II activity observed following normothermic ischemia is not seen under conditions of intraischemic hypothermia (57,110). Ubiquitin, a small protein involved in the catabolism of other abnormal proteins, is decreased following ischemia this may lead to an accumulation of abnormal proteins that affect cell function. Intraischemic hypothermia induces a significant restitution of ubiquitin compared to the normothermic condition (111). 

Fig. 2. Messengers mediating the initial and sustained phases of the All-induced cellular response. Initial phase All-elicited hydrolysis of PIP2 induces a transient rise in cytosolic calcium (via IP3), a transient activation of calcium-, calmodulin-dependent protein kinases, a transient increase in the phosphorylation of early-phase phosphoproteins (Pra-P), and a transient cellular response. Sustained response All-elicited hydrolysis of phosphoinositides generates a sustained increase in the diacylglycerol (DG) content of the plasma membrane. In conjunction with a sustained increase in plasma membrane calcium cycling, DG induces the sustained activation of protein kinase C (CK), the sustained increase in the phosphorylation of late-phase phosphoproteins (P -P) and the sustained cellular response.

McKinsey TA, Zhang CL, Olson EN (2000) Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5. Proc Natl Acad Sci USA 97(26) 14400-14405... 

Consensus sites for phosphorylation were evident in the neuronal NOS enzyme from the predicted protein sequences derived from cDNA analysis. In vitro biochemical studies indicate that nNOS can be phosphorylated by calcium/calmodulin-dependent protein kinase, cAMP-dependent protein kinase, cGMP-dependent protein kinase, and protein kinase C. Phosphorylation of nNOS by all of these enzymes decreases NOS catalytic activity in vitro (Dawson and Snyder, 1994 Bredt etal., 1992 Dinerman etal., 1994a). Calcineurin, a protein phosphatase, dephosphorylates NOS and subsequently increases its catalytic activity (T. M. Dawson etal., 1993). Multiple levels of constitutive nNOS regulation are thus possible by phosphorylation. 

Beg, Z.H. Stonik, J.A. Brewer, H.B. Phosphorylation and modulation of the enzymic activity of native and protease-cleaved purified hepatic 3-hy-droxy-3-methylglutaryl-coenzyme A reductase by a calcium/calmodulin-dependent protein kinase. J. Biol. Chem., 262, 13228-13240 (1987)... 

Atkins CM, Chen S, Alonso OF, Dietrich WD, Hu BR (2009a) Activation of calcium/calmodulin-dependent protein kinases after traumatic brain injury. J Cereb Blood Flow Metab 26 1507-1518... 

Major changes in phosphorylation induced by ischaemia and subsequent reperfusion in rat striatum were observed for a 130-kDa protein, tentatively identified as the Ca "" transport ATPase, and calcium/calmodulin-dependent protein kinase II (Sankaran etal. 1997). A 200-300% increase in [ PjSNjATP photoinsertions was observed in the striatum and hippocampus region of a 43-kDa protein with an isoelectric point of 6.8. This protein was identified as glutamine synthetase and the increase in binding was found to be due to both increased copy number and activation by Mn ". An increase in [ PjSNjATP photoinsertions into a 55-kDa protein, identified as the P-subunit of tubulin, was found only in the striatum and hippocampus indicating the depolymerization of microtubulin in these tissues. 

Jones TL, Lustig AC, Sorkin LS. Secondary hyperalgesia in the post-operative pain model is dependent on spinal calcium/calmodulin-dependent protein kinase II activation. Anesth Analg 2007 105 1650-1656. 

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