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Association of the Src homology 2 domain‐containing leukocyte phosphoprotein of 76 kD (SLP‐76) with the p85 subunit of phosphoinositide 3‐kinase
Author(s) -
Shim Eun Kyung,
Moon Chang Suk,
Lee Gi Yeon,
Ha Yun Jung,
Chae Suhn-Kee,
Lee Jong Ran
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.090
Subject(s) - phosphoinositide 3 kinase , phosphoprotein , proto oncogene tyrosine protein kinase src , protein subunit , microbiology and biotechnology , homology (biology) , chemistry , kinase , phosphorylation , biology , biochemistry , protein kinase b , amino acid , gene
To investigate additional functions of the T cell adaptor, Src homology 2 (SH2) domain‐containing leukocyte protein of 76 kD (SLP‐76), we performed a yeast two‐hybrid assay using the N‐terminal region of SLP‐76 fused with the kinase domain of Syk. By screening a human leukemia cDNA library, we identified the p85 subunit of phosphoinositide 3‐kinase (PI3K) as one of the interacting molecules. Unlike the SH2 domain of Vav or Nck, tyrosine phosphorylation of SLP‐76 at position 113 or 128 was sufficient for it to associate with the N‐terminal SH2 of p85. Collectively, these data suggest that SLP‐76 may play a role in PI3K signaling pathways.