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rdf:type |
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lifeskim:mentions |
umls-concept:C0010656,
umls-concept:C0033684,
umls-concept:C0205314,
umls-concept:C0271510,
umls-concept:C0332256,
umls-concept:C0679622,
umls-concept:C0766164,
umls-concept:C1334043,
umls-concept:C1367449,
umls-concept:C1514562,
umls-concept:C1706590,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697616
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pubmed:issue |
15
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pubmed:dateCreated |
1999-5-3
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pubmed:databankReference |
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pubmed:abstractText |
We have identified and characterized CIPER, a novel protein containing a caspase recruitment domain (CARD) in its N terminus and a C-terminal region rich in serine and threonine residues. The CARD of CIPER showed striking similarity to E10, a product of the equine herpesvirus-2. CIPER formed homodimers via its CARD and interacted with viral E10 but not with several apoptosis regulators containing CARDs including ARC, RAIDD, RICK, caspase-2, caspase-9, or Apaf-1. Expression of CIPER induced NF-kappaB activation, which was inhibited by dominant-negative NIK and a nonphosphorylable IkappaB-alpha mutant but not by dominant-negative RIP. Mutational analysis revealed that the N-terminal region of CIPER containing the CARD was sufficient and necessary for NF-kappaB-inducing activity. Point mutations in highly conserved residues in the CARD of CIPER disrupted the ability of CIPER to activate NF-kappaB and to form homodimers, indicating that the CARD is essential for NF-kappaB activation and dimerization. We propose that CIPER acts in a NIK-dependent pathway of NF-kappaB activation.
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pubmed:grant |
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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/APAF1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Apaf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptotic Protease-Activating...,
http://linkedlifedata.com/resource/pubmed/chemical/BCL10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bcl10 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ced-3 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9955-61
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pubmed:dateRevised |
2008-9-26
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pubmed:meshHeading |
pubmed-meshheading:10187770-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10187770-Amino Acid Sequence,
pubmed-meshheading:10187770-Animals,
pubmed-meshheading:10187770-Apoptosis,
pubmed-meshheading:10187770-Apoptotic Protease-Activating Factor 1,
pubmed-meshheading:10187770-Blotting, Northern,
pubmed-meshheading:10187770-Caenorhabditis elegans Proteins,
pubmed-meshheading:10187770-Carrier Proteins,
pubmed-meshheading:10187770-Caspase 2,
pubmed-meshheading:10187770-Caspase 9,
pubmed-meshheading:10187770-Caspases,
pubmed-meshheading:10187770-Cysteine Endopeptidases,
pubmed-meshheading:10187770-Enzyme Activation,
pubmed-meshheading:10187770-Expressed Sequence Tags,
pubmed-meshheading:10187770-Humans,
pubmed-meshheading:10187770-Jurkat Cells,
pubmed-meshheading:10187770-Mice,
pubmed-meshheading:10187770-Molecular Sequence Data,
pubmed-meshheading:10187770-NF-kappa B,
pubmed-meshheading:10187770-Neoplasm Proteins,
pubmed-meshheading:10187770-Point Mutation,
pubmed-meshheading:10187770-Proteins,
pubmed-meshheading:10187770-Sequence Homology, Amino Acid
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pubmed:year |
1999
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pubmed:articleTitle |
CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10.
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pubmed:affiliation |
Department of Pathology and Comprehensive Cancer Center, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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