RGSZ2 Binds to the Neural Nitric Oxide Synthase PDZ Domain to Regulate Mu-Opioid Receptor-Mediated Potentiation of the N-Methyl-D-Aspartate Receptor-Calmodulin-Dependent Protein Kinase II Pathway

2011 ◽  
Vol 15 (4) ◽  
pp. 873-887 ◽  
Author(s):  
Javier Garzón ◽  
María Rodríguez-Muñoz ◽  
Ana Vicente-Sánchez ◽  
Concha Bailón ◽  
Ricardo Martínez-Murillo ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Pdz Domain ◽  
Mu Opioid Receptor ◽  
Dependent Protein Kinase ◽  
Mu Opioid ◽  
Aspartate Receptor ◽  
Dependent Protein ◽  
Neural Nitric Oxide Synthase ◽  
Oxide Synthase

scholarly journals Coordination between Calcium/Calmodulin-Dependent Protein Kinase II and Neuronal Nitric Oxide Synthase in Neurons

2020 ◽  
Vol 21 (21) ◽  
pp. 7997
Author(s):  
Shoma Araki ◽  
Koji Osuka ◽  
Tsuyoshi Takata ◽  
Yukihiro Tsuchiya ◽  
Yasuo Watanabe
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Cell Injury ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
Pathophysiological Role ◽  
Protein Kinase Ii ◽  
Mutual Regulation ◽  
Dependent Protein ◽  
Oxide Synthase

Ca2+/calmodulin (CaM)-dependent protein kinase II (CaMKII) is highly abundant in the brain and exhibits broad substrate specificity, thereby it is thought to participate in the regulation of neuronal death and survival. Nitric oxide (NO), produced by neuronal NO synthase (nNOS), is an important neurotransmitter and plays a role in neuronal activity including learning and memory processes. However, high levels of NO can contribute to excitotoxicity following a stroke and neurodegenerative disease. Aside from NO, nNOS also generates superoxide which is involved in both cell injury and signaling. CaMKII is known to activate and translocate from the cytoplasm to the post-synaptic density in response to neuronal activation where nNOS is predominantly located. Phosphorylation of nNOS at Ser847 by CaMKII decreases NO generation and increases superoxide generation. Conversely, NO-induced S-nitrosylation of CaMKII at Cys6 is a prominent determinant of the CaMKII inhibition in ATP competitive fashion. Thus, the “cross-talk” between CaMKII and NO/superoxide may represent important signal transduction pathways in brain. In this review, we introduce the molecular mechanism of and pathophysiological role of mutual regulation between CaMKII and nNOS in neurons.

scholarly journals Neuronal Nitric Oxide Synthase and Calmodulin-Dependent Protein Kinase IIα Undergo Neurotoxin-Induced Proteolysis

2002 ◽  
Vol 69 (3) ◽  
pp. 1006-1013 ◽  
Author(s):  
Iradj Hajimohammadreza ◽  
Kadee J. Raser ◽  
Rathna Nath ◽  
Ravi Nadimpalli ◽  
Michele Scott ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Kinase ◽  
Nitric Oxide Synthase ◽  
Neuronal Nitric Oxide Synthase ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Oxide Synthase
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