| pubmed-article:17052756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17052756 | lifeskim:mentions | umls-concept:C0248868 | lld:lifeskim |
| pubmed-article:17052756 | lifeskim:mentions | umls-concept:C1367449 | lld:lifeskim |
| pubmed-article:17052756 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:17052756 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:17052756 | pubmed:dateCreated | 2006-12-4 | lld:pubmed |
| pubmed-article:17052756 | pubmed:abstractText | Ordered assembly of scaffold proteins Carma1-Bcl10-Malt1 determines NF-kappaB activation following T cell receptor (TCR) engagement. Carma1-Bcl10 interaction and the signaling pathway are controlled by Carma1 phosphorylation, which are induced by PKCtheta and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). In addition to Carma1 phosphorylation, previous studies have demonstrated that Bcl10 is phosphorylated in the C-terminal Ser/Thr rich region following TCR engagement. However the kinases that phosphorylate Bcl10 are incompletely understood. Here we show that CaMKII phosphorylates Bcl10 on Ser138. Furthermore, a CaMKII inhibitor, KN93, and CaMKII siRNA substantially reduce Bcl10 phosphorylation induced by phorbol myristate acetate/ionomycin. S138A mutation prolongs Bcl10-induced NF-kappaB activation, suggesting that Bcl10 phosphorylation is involved in attenuation of NF-kappaB activation. These findings suggest that CaMKII modulates NF-kappaB activation via phosphorylating Bcl10 as well as Carma1. | lld:pubmed |
| pubmed-article:17052756 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17052756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17052756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17052756 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17052756 | pubmed:issn | 0161-5890 | lld:pubmed |
| pubmed-article:17052756 | pubmed:author | pubmed-author:GotoHidemiH | lld:pubmed |
| pubmed-article:17052756 | pubmed:author | pubmed-author:AndoTakafumiT | lld:pubmed |
| pubmed-article:17052756 | pubmed:author | pubmed-author:XavierRamnikR | lld:pubmed |
| pubmed-article:17052756 | pubmed:author | pubmed-author:IshiguroKazuh... | lld:pubmed |
| pubmed-article:17052756 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17052756 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:17052756 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17052756 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17052756 | pubmed:pagination | 2095-100 | lld:pubmed |
| pubmed-article:17052756 | pubmed:dateRevised | 2011-10-31 | lld:pubmed |
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| pubmed-article:17052756 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17052756 | pubmed:articleTitle | Bcl10 is phosphorylated on Ser138 by Ca2+/calmodulin-dependent protein kinase II. | lld:pubmed |
| pubmed-article:17052756 | pubmed:affiliation | Molecular Biology and Pathogenesis of Gastroenterology, Nagoya University School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya, Aichi 466-8550, Japan. kio@med.nagoya-u.ac.jp | lld:pubmed |
| pubmed-article:17052756 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:815 | entrezgene:pubmed | pubmed-article:17052756 | lld:entrezgene |
| entrez-gene:8915 | entrezgene:pubmed | pubmed-article:17052756 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17052756 | lld:pubmed |
