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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2002-6-18
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10195894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10352268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10637282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10648608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10811866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10811867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10820247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-10837071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11181694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11283593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11444380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11520989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11562344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11598012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11875461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-11976686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-7642213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-7897216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-8657279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-8670417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-8717510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-8855292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-8887559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9081673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9323135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9429891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9653087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9722915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9736610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12070292-9744859
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chuk protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Ikbkb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ikbke protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C beta
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1647-52
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12070292-Animals,
pubmed-meshheading:12070292-B-Lymphocytes,
pubmed-meshheading:12070292-I-kappa B Kinase,
pubmed-meshheading:12070292-Isoenzymes,
pubmed-meshheading:12070292-Mice,
pubmed-meshheading:12070292-Mice, Inbred C57BL,
pubmed-meshheading:12070292-NF-kappa B,
pubmed-meshheading:12070292-Phosphorylation,
pubmed-meshheading:12070292-Protein Kinase C,
pubmed-meshheading:12070292-Protein-Serine-Threonine Kinases
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pubmed:year |
2002
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pubmed:articleTitle |
Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha.
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pubmed:affiliation |
Laboratory of Lymphocyte Signaling, Rockefeller University, New York, NY 10021, USA. saijok@mail.rockefeller.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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