RRC ID 38847
著者 Takemoto Y, Sato M, Furuta M, Hashimoto Y.
タイトル Distinct binding patterns of HS1 to the Src SH2 and SH3 domains reflect possible mechanisms of recruitment and activation of downstream molecules.
ジャーナル Int Immunol
Abstract We previously identified a gene, LckBP1, which encodes a protein that binds to the Lck SH3 domain and is identical to murine SH1. Using unstimulated T lymphocytes, we further demonstrated that Lck binds to HS1 in vivo and that HS1 is tyrosine phosphorylated upon TCR stimulation. In the present report, we analyzed the binding pattern of several src kinases and HS1 in greater detail. The Lck SH3 domain binds to HS1 constitutively, while the Lck SH2 domain associates with HS1 only upon TCR stimulation. A similar binding pattern was observed with Lyn and HS1, but not with Fyn and HS1, in which the Fyn SH2 region associates with HS1 upon TCR stimulation but the Fyn SH3 region does not associate with HS1 regardless of TCR stimulation. Such distinct binding patterns of the src kinase SH2 and SH3 domains to HS1 may represent a mechanism by which src family kinases select substrates and activate particular downstream signaling pathways.
巻・号 8(11)
ページ 1699-705
公開日 1996-11-1
DOI 10.1093/intimm/8.11.1699
PMID 8943564
MeSH Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Blood Proteins / metabolism* Enzyme Activation / immunology Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Mice Molecular Sequence Data Protein Binding / immunology Protein Structure, Tertiary Signal Transduction / immunology T-Lymphocytes / immunology src Homology Domains / immunology* src-Family Kinases / metabolism
IF 3.519
引用数 33
WOS 分野 IMMUNOLOGY
リソース情報
ヒト・動物細胞 NIH3T3-3(RCB0150)