| pubmed-article:12630910 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12630910 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:12630910 | lifeskim:mentions | umls-concept:C0669368 | lld:lifeskim |
| pubmed-article:12630910 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:12630910 | lifeskim:mentions | umls-concept:C0769224 | lld:lifeskim |
| pubmed-article:12630910 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:12630910 | pubmed:dateCreated | 2003-5-21 | lld:pubmed |
| pubmed-article:12630910 | pubmed:abstractText | Post-synaptic density-95 (PSD-95) is a neuronal scaffolding protein that associates with N -methyl-D-aspartate (NMDA) receptors and links them to intracellular signalling molecules. In neurons, neuronal nitric oxide synthase (nNOS) binds selectively to the second PDZ domain (PDZ2) of PSD-95, thereby exhibiting physiological activation triggered via NMDA receptors. We have demonstrated previously that Ca(2+)/calmodulin-dependent protein kinase IIalpha (CaM-K IIalpha) directly phosphorylates nNOS at residue Ser(847), and can attenuate the catalytic activity of the enzyme in neuronal cells [Komeima, Hayashi, Naito and Watanabe (2000) J. Biol. Chem. 275, 28139-28143]. In the present study, we examined how CaM-K II participates in the phosphorylation by analysing the functional interaction between nNOS and PSD-95 in cells. The results showed that PSD-95 directly promotes the nNOS phosphorylation at Ser(847) induced by endogenous CaM-K II. In transfected cells, this effect of PSD-95 required its dual palmitoylation and the PDZ2 domain, but did not rely on its guanylate kinase domain. CaM-K Ialpha and CaM-K IV failed to phosphorylate nNOS at Ser(847) in transfected cells. Thus PSD-95 mediates cellular trafficking of nNOS, and may be required for the efficient phosphorylation of nNOS at Ser(847) by CaM-K II in neuronal cells. | lld:pubmed |
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| pubmed-article:12630910 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12630910 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12630910 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12630910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12630910 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12630910 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12630910 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:SorkV LVL | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:YamamotoTadas... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:TezukaTohruT | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:WatanabeYasuo... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:SugimotoKatsu... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:TokudaMasaaki... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:TokumitsuHiro... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:ArakiNobukazu... | lld:pubmed |
| pubmed-article:12630910 | pubmed:author | pubmed-author:HoriiMarikoM | lld:pubmed |
| pubmed-article:12630910 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12630910 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12630910 | pubmed:volume | 372 | lld:pubmed |
| pubmed-article:12630910 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12630910 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12630910 | pubmed:pagination | 465-71 | lld:pubmed |
| pubmed-article:12630910 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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