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 language | English |
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Pages (from-to) | 35-40 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 575 |
Issue number | 1-3 |
DOIs | |
State | Published - 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