Association of the Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD (SLP-76) with the p85 subunit of phosphoinositide 3-kinase
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.
- Publication:
-
FEBS Letters
- Pub Date:
- January 2004
- DOI:
- 10.1016/j.febslet.2004.07.090
- Bibcode:
- 2004FEBSL.575...35S
- Keywords:
-
- SH2;
- Src homology 2;
- SLP-76;
- Src homology 2 domain-containing leukocyte phosphoprotein of 76 kD;
- PI3K;
- phosphoinositide 3-kinase;
- PTK;
- protein tyrosine kinase;
- TCR;
- T cell receptor;
- Ab;
- antibody;
- IP;
- immunoprecipitation;
- IB;
- immunoblotting;
- WT;
- wild-type;
- GST;
- glutathione S-transferase;
- HEK;
- human embryonic kidney;
- PV;
- pervanadate;
- Src homology 2 domain-containing leukocyte protein of 76 kD;
- Adaptor protein;
- Yeast two-hybrid screening;
- Phosphoinositide 3-kinase;
- Tyrosine phosphorylation;
- Src homology 2 domain