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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2003-3-24
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pubmed:databankReference |
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pubmed:abstractText |
As a c-fms-interacting protein, we cloned a novel adaptor molecule, signal-transducing adaptor protein-2 (STAP-2), which contains pleckstrin homology- and Src homology 2-like (PH and SRC) domains and a proline-rich region. STAP-2 is structurally related to STAP-1/BRDG1 (BCR downstream signaling-1), which we had cloned previously from hematopoietic stem cells. STAP-2 is a murine homologue of a recently identified adaptor molecule, BKS, a substrate of BRK tyrosine kinase. STAP-2 was tyrosine-phosphorylated and translocated to the plasma membrane in response to epidermal growth factor when overexpressed in fibroblastic cells. To define the function of STAP-2, we generated mice lacking the STAP-2 gene. STAP-2 mRNA was strongly induced in the liver in response to lipopolysaccharide and in isolated hepatocytes in response to interleukin-6. In the STAP-2(-/-) hepatocytes, the interleukin-6-induced expression of acute-phase (AP) genes and the tyrosine-phosphorylation level of STAT3 were reduced specifically at the late phase (6-24 h) of the response. These data indicate that STAP-2 plays a regulatory role in the AP response in systemic inflammation. STAP-2 contains a YXXQ motif in the C-terminal region that is a potential STAT3-binding site. Overexpression of wild-type STAP-2, but not of mutants lacking this motif, enhanced the AP response element reporter activity and an AP protein production. These data suggest that STAP-2 is a new class of adaptor molecule that modulates STAT3 activity through its YXXQ motif.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/STAP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/STAT3 Transcription Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Stat3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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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 |
28
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11182-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12540842-Acute-Phase Reaction,
pubmed-meshheading:12540842-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12540842-Amino Acid Motifs,
pubmed-meshheading:12540842-Amino Acid Sequence,
pubmed-meshheading:12540842-Animals,
pubmed-meshheading:12540842-Base Sequence,
pubmed-meshheading:12540842-Blotting, Northern,
pubmed-meshheading:12540842-Cell Membrane,
pubmed-meshheading:12540842-DNA Primers,
pubmed-meshheading:12540842-DNA-Binding Proteins,
pubmed-meshheading:12540842-Gene Expression Regulation,
pubmed-meshheading:12540842-Mice,
pubmed-meshheading:12540842-Molecular Sequence Data,
pubmed-meshheading:12540842-Phosphoproteins,
pubmed-meshheading:12540842-Phosphorylation,
pubmed-meshheading:12540842-Precipitin Tests,
pubmed-meshheading:12540842-RNA, Messenger,
pubmed-meshheading:12540842-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12540842-STAT3 Transcription Factor,
pubmed-meshheading:12540842-Sequence Homology, Amino Acid,
pubmed-meshheading:12540842-Trans-Activators,
pubmed-meshheading:12540842-Tyrosine
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pubmed:year |
2003
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pubmed:articleTitle |
STAP-2/BKS, an adaptor/docking protein, modulates STAT3 activation in acute-phase response through its YXXQ motif.
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pubmed:affiliation |
Division of Molecular and Cellular Immunology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashiku, Fukuoka 812-8582, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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