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rdf:type |
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lifeskim:mentions |
umls-concept:C0015576,
umls-concept:C0031727,
umls-concept:C0079904,
umls-concept:C0162638,
umls-concept:C0205314,
umls-concept:C0679622,
umls-concept:C0680022,
umls-concept:C1150524,
umls-concept:C1335623,
umls-concept:C1415715,
umls-concept:C1515877,
umls-concept:C1522240,
umls-concept:C1538842,
umls-concept:C1879547
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pubmed:issue |
12
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pubmed:dateCreated |
2002-12-11
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pubmed:abstractText |
RIP1 and its homologs, RIP2 and RIP3, form part of a family of Ser/Thr kinases that regulate signal transduction processes leading to NF-kappa B activation. Here, we identify RIP4 (DIK/PKK) as a novel member of the RIP kinase family. RIP4 contains an N-terminal RIP-like kinase domain and a C-terminal region characterized by the presence of 11 ankyrin repeats. Overexpression of RIP4 leads to activation of NF-kappa B and JNK. Kinase inactive RIP4 or a truncated version containing the ankyrin repeats have a dominant negative (DN) effect on NF-kappa B induction by multiple stimuli. RIP4 binds to several members of the TRAF protein family, and DN versions of TRAF1, TRAF3 and TRAF6 inhibit RIP4-induced NF-kappa B activation. Moreover, RIP4 is cleaved after Asp340 and Asp378 during Fas-induced apoptosis. These data suggest that RIP4 is involved in NF-kappa B and JNK signaling and that caspase-dependent processing of RIP4 may negatively regulate NF-kappa B-dependent pro-survival or pro-inflammatory signals.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10339433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10358032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10442092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10521396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10692573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10723801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10818227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10880512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-10948194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-11278382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-11734559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-11875461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-11894097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-11894098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-7768349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-8612133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-8867839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-8947041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-9529147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-9575181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-9642260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12446564-9705938
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1201-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-kappa B and is processed during apoptosis.
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pubmed:affiliation |
Institute of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, CH-1066 Epalinges, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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