FEBS Letters · 2004 · 32 citations · 27 references
Life SciencesBiochemistryMolecular BiologyCell SignalingMolecular Cell BiologySignal TransductionAdaptor Protein ComplexesPhosphoinositide SignalingProtein Kinase CascadesProtein PhosphorylationReceptor Tyrosine Kinase SignalingKinase DomainsPhosphatidylinositol 3-Kinase PathwayPhosphoinositide 3-Kinase SignalingPi3k SignalingProtein Tyrosine PhosphorylationSh2 Domain-mediated SignalingSh2 DomainsSrc Homology 2 Domains
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.
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