| pubmed-article:17442679 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17442679 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:17442679 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:17442679 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:17442679 | lifeskim:mentions | umls-concept:C0034807 | lld:lifeskim |
| pubmed-article:17442679 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:17442679 | pubmed:dateCreated | 2007-6-11 | lld:pubmed |
| pubmed-article:17442679 | pubmed:abstractText | Phosphorylation can affect both the function and trafficking of GABA(A) receptors with significant consequences for neuronal excitability. Serine/threonine kinases can phosphorylate the intracellular loops between M3-4 of GABA(A) receptor beta and gamma subunits thereby modulating receptor function in heterologous expression systems and in neurons (1, 2). Specifically, CaMK-II has been demonstrated to phosphorylate the M3-4 loop of GABA(A) receptor subunits expressed as GST fusion proteins (3, 4). It also increases the amplitude of GABA(A) receptor-mediated currents in a number of neuronal cell types (5-7). To identify which substrate sites CaMK-II might phosphorylate and the consequent functional effects, we expressed recombinant GABA(A) receptors in NG108-15 cells, which have previously been shown to support CaMK-II modulation of GABA(A) receptors containing the beta3 subunit (8). We now demonstrate that CaMK-II mediates its effects on alpha1beta3 receptors via phosphorylation of Ser(383) within the M3-4 domain of the beta subunit. Ablation of beta3 subunit phosphorylation sites for CaMK-II revealed that for alphabetagamma receptors, CaMK-II has a residual effect on GABA currents that is not mediated by previously identified sites of CaMK-II phosphorylation. This residual effect is abolished by mutation of tyrosine phosphorylation sites, Tyr(365) and Tyr(367), on the gamma2S subunit, and by the tyrosine kinase inhibitor genistein. These results suggested that CaMK-II is capable of directly phosphorylating GABA(A) receptors and activating endogenous tyrosine kinases to phosphorylate the gamma2 subunit in NG108-15 cells. These findings were confirmed in a neuronal environment by expressing recombinant GABA(A) receptors in cerebellar granule neurons. | lld:pubmed |
| pubmed-article:17442679 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442679 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17442679 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17442679 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17442679 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17442679 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17442679 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17442679 | pubmed:author | pubmed-author:MossStephen... | lld:pubmed |
| pubmed-article:17442679 | pubmed:author | pubmed-author:HosieAlastair... | lld:pubmed |
| pubmed-article:17442679 | pubmed:author | pubmed-author:SmartTrevor... | lld:pubmed |
| pubmed-article:17442679 | pubmed:author | pubmed-author:LeeHenry H... | lld:pubmed |
| pubmed-article:17442679 | pubmed:author | pubmed-author:HoustonCatrio... | lld:pubmed |
| pubmed-article:17442679 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17442679 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17442679 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17442679 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17442679 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17442679 | pubmed:pagination | 17855-65 | lld:pubmed |
| pubmed-article:17442679 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:17442679 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17442679 | pubmed:articleTitle | Identification of the sites for CaMK-II-dependent phosphorylation of GABA(A) receptors. | lld:pubmed |
| pubmed-article:17442679 | pubmed:affiliation | Department of Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom. | lld:pubmed |
| pubmed-article:17442679 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17442679 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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