Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase

Eun Kyung Shim, Chang Suk Moon, Gi Yeon Lee, Yun Jung Ha, Suhn Kee Chae, Jong Ran Lee

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)35-40
Number of pages6
JournalFEBS Letters
Volume575
Issue number1-3
DOIs
StatePublished - 24 Sep 2004

Keywords

  • Ab, antibody
  • IB, immunoblotting
  • IP, immunoprecipitation
  • PI3K, phosphoinositide 3-kinase
  • PTK, protein tyrosine kinase
  • SH2, Src homology 2
  • SLP-76, Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD
  • TCR, T cell receptor
  • WT, wild-type

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