Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.

This study addresses the interactions between the adaptor protein Shb and components involved in T cell signalling, including SLP-76, Gads, Vav and ZAP70. We show that both SLP-76 and ZAP70 co-immunoprecipitate with Shb in Jurkat T cells and that Shb and Vav co-immunoprecipitate when cotransfected in COS cells. We also ...
demonstrate, utilizing fusion protein constructs, that SLP-76, Gads and Vav associate independently of each other to different domains or regions, of Shb. Overexpression of an SH2 domain-defective Shb causes diminished phosphorylation of SLP-76 and Vav and consequently decreased activation of c-Jun kinase upon T cell receptor (TCR) stimulation. Shb was also found to localize to glycolipid-enriched membrane microdomains (GEMs), also called lipid rafts, after TCR stimulation. Our results indicate that upon TCR stimulation, Shb is targeted to these lipid rafts where Shb aids in recruiting the SLP-76-Gads-Vav complex to the T cell receptor zeta-chain and ZAP70.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antigens, CD3, COS Cells, Carrier Proteins, Cell Membrane, Humans, JNK Mitogen-Activated Protein Kinases, Jurkat Cells, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Oncogene Proteins, Phosphoproteins, Phosphorylation, Point Mutation, Precipitin Tests, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-vav, Receptors, Antigen, T-Cell, Recombinant Fusion Proteins, Signal Transduction, Tyrosine, ZAP-70 Protein-Tyrosine Kinase, rac1 GTP-Binding Protein, src Homology Domains
Eur. J. Biochem.
Date: Jul. 01, 2002
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