| pubmed-article:12070292 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C0754623 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C0257291 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12070292 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12070292 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:12070292 | pubmed:dateCreated | 2002-6-18 | lld:pubmed |
| pubmed-article:12070292 | pubmed:abstractText | Activation of the nuclear factor (NF)-kappaB transcription complex by signals derived from the surface expressed B cell antigen receptor controls B cell development, survival, and antigenic responses. Activation of NF-kappaB is critically dependent on serine phosphorylation of the IkappaB protein by the multi-component IkappaB kinase (IKK) containing two catalytic subunits (IKKalpha and IKKbeta) and one regulatory subunit (IKKgamma). Using mice deficient for protein kinase C beta (PKCbeta) we show an essential role of PKCbeta in the phosphorylation of IKKalpha and the subsequent activation of NF-kappaB in B cells. Defective IKKalpha phosphorylation correlates with impaired B cell antigen receptor-mediated induction of the pro-survival protein Bcl-xL. Lack of IKKalpha phosphorylation and defective NF-kappaB induction in the absence of PKCbeta explains the similarity in immunodeficiencies caused by PKCbeta or IKKalpha ablation in B cells. Furthermore, the well established functional cooperation between the protein tyrosine kinase Bruton's tyrosine kinase (Btk), which regulates the activity of NF-kappaB and PKCbeta, suggests PKCbeta as a likely serine/threonine kinase component of the Btk-dependent NF-kappaB activating signal transduction chain downstream of the BCR. | lld:pubmed |
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| pubmed-article:12070292 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12070292 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12070292 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12070292 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12070292 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:12070292 | pubmed:author | pubmed-author:TarakhovskyAl... | lld:pubmed |
| pubmed-article:12070292 | pubmed:author | pubmed-author:SaijoKaoruK | lld:pubmed |
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| pubmed-article:12070292 | pubmed:author | pubmed-author:LeitgerMichae... | lld:pubmed |
| pubmed-article:12070292 | pubmed:author | pubmed-author:SchmedtChrist... | lld:pubmed |
| pubmed-article:12070292 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12070292 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:12070292 | pubmed:volume | 195 | lld:pubmed |
| pubmed-article:12070292 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12070292 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12070292 | pubmed:pagination | 1647-52 | lld:pubmed |
| pubmed-article:12070292 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12070292 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12070292 | pubmed:articleTitle | Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha. | lld:pubmed |
| pubmed-article:12070292 | pubmed:affiliation | Laboratory of Lymphocyte Signaling, Rockefeller University, New York, NY 10021, USA. saijok@mail.rockefeller.edu | lld:pubmed |
| pubmed-article:12070292 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12070292 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12070292 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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