Source:http://linkedlifedata.com/resource/pubmed/id/10497204
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
40
|
| pubmed:dateCreated |
1999-11-2
|
| pubmed:databankReference | |
| pubmed:abstractText |
T-cell activation involves the participation of protein-tyrosine kinases p56(lck) and ZAP-70/SYK as well as lymphoid proteins such as SLP-76 and FYB/SLAP. FYB/SLAP has the hallmarks of an adaptor protein that binds to the SH2 domains of the Src kinase FYN-T and SLP-76. Whereas two forms of FYB at 120 and 130 kDa have been identified biochemically, a cDNA encoding only the lower molecular weight isoform has been cloned (termed FYB-120 or SLAP-130). In this study, we report the isolation of an alternative isoform of FYB with a molecular mass of 130 kDa (FYB-130) that has the same structure as FYB-120 except for an insertion of 46 amino acids toward the carboxyl-terminal region of the protein. FYB-120 and FYB-130 share an ability to bind to the SH2 domains of FYN-T and SLP-76, to act as substrates for p59(FYN-T), and to be expressed in the cytoplasm and nucleus of T-cells. Differences were noted between the isoforms in the efficiency of binding to SLP-76 and in the preferential expression of FYB-130 in mature T-cells. When co-expressed together with FYN-T and SLP-76, FYB-130 caused a significant increase in anti-CD3-driven NF-AT transcription. Finally, fluorescence in situ hybridization analysis localized the FYB gene to human chromosome 5 at position p13.1. FYB-130 therefore represents a novel variant of FYB protein that can up-regulate T-cell receptor-driven interleukin 2 production in mature T-cells.
|
| 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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FYB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/SLP-76 signal Transducing adaptor...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
28427-35
|
| pubmed:dateRevised |
2006-9-29
|
| pubmed:meshHeading |
pubmed-meshheading:10497204-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10497204-Amino Acid Sequence,
pubmed-meshheading:10497204-Base Sequence,
pubmed-meshheading:10497204-Carrier Proteins,
pubmed-meshheading:10497204-Cell Nucleus,
pubmed-meshheading:10497204-Chromosome Mapping,
pubmed-meshheading:10497204-Chromosomes, Human, Pair 5,
pubmed-meshheading:10497204-Cloning, Molecular,
pubmed-meshheading:10497204-Cytoplasm,
pubmed-meshheading:10497204-Humans,
pubmed-meshheading:10497204-Interleukin-2,
pubmed-meshheading:10497204-Molecular Sequence Data,
pubmed-meshheading:10497204-Phosphoproteins,
pubmed-meshheading:10497204-Protein Binding,
pubmed-meshheading:10497204-Protein Isoforms,
pubmed-meshheading:10497204-Sequence Homology, Amino Acid,
pubmed-meshheading:10497204-T-Lymphocytes,
pubmed-meshheading:10497204-Thymus Gland,
pubmed-meshheading:10497204-Up-Regulation
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production.
|
| pubmed:affiliation |
Department of Cancer Immunology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
|
| pubmed:publicationType |
Journal Article
|