|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6730
|
|
pubmed:dateCreated |
1999-6-14
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Fas is a cell-surface receptor molecule that relays apoptotic (cell death) signals into cells. When Fas is activated by binding of its ligand, the proteolytic protein caspase-8 is recruited to a signalling complex known as DISC by binding to a Fas-associated adapter protein. A large new protein, FLASH, has now been identified by cloning of its complementary DNA. This protein contains a motif with oligomerizing activity whose sequence is similar to that of the Caenorhabditis elegans protein CED-4, and another domain (DRD domain) that interacts with a death-effector domain in caspase-8 or in the adapter protein. Stimulated Fas binds FLASH, so FLASH is probably a component of the DISC signalling complex. Transient expression of FLASH activates caspase-8, whereas overexpression of a truncated form of FLASH containing only one of its DRD or CED-4-like domains does not allow activation of caspase-8 and Fas-mediated apoptosis to occur. Overexpression of full-length FLASH blocks the anti-apoptotic effect of the adenovirus protein E1B19K. FLASH is therefore necessary for the activation of caspase-8 in Fas-mediated apoptosis.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus E1 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8AP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Casp8 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp8ap2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Ced-4 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fadd protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0028-0836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
29
|
|
pubmed:volume |
398
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
777-85
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10235259-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10235259-Adenovirus E1 Proteins,
pubmed-meshheading:10235259-Amino Acid Sequence,
pubmed-meshheading:10235259-Animals,
pubmed-meshheading:10235259-Antigens, CD95,
pubmed-meshheading:10235259-Apoptosis,
pubmed-meshheading:10235259-Apoptosis Regulatory Proteins,
pubmed-meshheading:10235259-Caenorhabditis elegans,
pubmed-meshheading:10235259-Caenorhabditis elegans Proteins,
pubmed-meshheading:10235259-Calcium-Binding Proteins,
pubmed-meshheading:10235259-Carrier Proteins,
pubmed-meshheading:10235259-Caspase 8,
pubmed-meshheading:10235259-Caspase 9,
pubmed-meshheading:10235259-Caspases,
pubmed-meshheading:10235259-Cell Line,
pubmed-meshheading:10235259-Cloning, Molecular,
pubmed-meshheading:10235259-Consensus Sequence,
pubmed-meshheading:10235259-Enzyme Activation,
pubmed-meshheading:10235259-Fas-Associated Death Domain Protein,
pubmed-meshheading:10235259-Helminth Proteins,
pubmed-meshheading:10235259-Humans,
pubmed-meshheading:10235259-Jurkat Cells,
pubmed-meshheading:10235259-Macromolecular Substances,
pubmed-meshheading:10235259-Mice,
pubmed-meshheading:10235259-Molecular Sequence Data,
pubmed-meshheading:10235259-Sequence Homology, Amino Acid,
pubmed-meshheading:10235259-Signal Transduction
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis.
|
|
pubmed:affiliation |
Institute for Virus Research, Kyoto University, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
