|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0010656,
umls-concept:C0033640,
umls-concept:C0162638,
umls-concept:C0205314,
umls-concept:C0271510,
umls-concept:C0332256,
umls-concept:C0679622,
umls-concept:C0851285,
umls-concept:C1335624,
umls-concept:C1413357,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
|
pubmed:issue |
20
|
|
pubmed:dateCreated |
1998-6-12
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Signaling through the CD95/Fas/APO-1 death receptor plays a critical role in the homeostasis of the immune system. RICK, a novel protein kinase that regulates CD95-mediated apoptosis was identified and characterized. RICK is composed of an N-terminal serine-threonine kinase catalytic domain and a C-terminal region containing a caspase-recruitment domain. RICK physically interacts with CLARP, a caspase-like molecule known to bind to Fas-associated protein with death domain (FADD) and caspase-8. Expression of RICK promoted the activation of caspase-8 and potentiated apoptosis induced by Fas ligand, FADD, CLARP, and caspase-8. Deletion mutant analysis revealed that both the kinase domain and caspase-recruitment domain were required for RICK to promote apoptosis. Significantly, expression of a RICK mutant in which the lysine of the putative ATP-binding site at position 38 was replaced by a methionine functioned as an inhibitor of CD95-mediated apoptosis. Thus, RICK represents a novel kinase that may regulate apoptosis induced by the CD95/Fas receptor pathway.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 and FADD-Like Apoptosis...,
http://linkedlifedata.com/resource/pubmed/chemical/CFLAR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
273
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
12296-300
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9575181-Adenosine Triphosphate,
pubmed-meshheading:9575181-Amino Acid Sequence,
pubmed-meshheading:9575181-Antigens, CD95,
pubmed-meshheading:9575181-Apoptosis,
pubmed-meshheading:9575181-Binding Sites,
pubmed-meshheading:9575181-CASP8 and FADD-Like Apoptosis Regulating Protein,
pubmed-meshheading:9575181-Cysteine Endopeptidases,
pubmed-meshheading:9575181-DNA, Complementary,
pubmed-meshheading:9575181-Humans,
pubmed-meshheading:9575181-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9575181-Molecular Sequence Data,
pubmed-meshheading:9575181-Mutagenesis,
pubmed-meshheading:9575181-Protein Binding,
pubmed-meshheading:9575181-Protein Kinases,
pubmed-meshheading:9575181-Proteins,
pubmed-meshheading:9575181-Receptor-Interacting Protein Serine-Threonine Kinase 2,
pubmed-meshheading:9575181-Sequence Deletion,
pubmed-meshheading:9575181-Sequence Homology, Amino Acid
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis.
|
|
pubmed:affiliation |
Department of Pathology and Comprehensive Cancer Center, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
