Product Reference
Interplay between the heterotrimeric G-protein subunits Galphaq and Galphai2 sets the threshold for chemotaxis and TCR activation.
| |
|
| Author |
Jacob Ngai,Marit Inngjerdingen,Torunn Berge,Kjetil Taskén |
| Citation Information |
BMC immunology, 10: (2009) |
| Keywords |
Chemokine CXCL12,Chemotaxis,Feedback, Physiological,GTP-Binding Protein alpha Subunit, Gi2,GTP-Binding Protein alpha Subunits, Gq-G11,Humans,Jurkat Cells,Lymphocyte Activation,Lymphocyte Specific Protein Tyrosine Kinase p56(lck),Protein Tyrosine Phosphatase, Non-Receptor Type 6,Receptors, Antigen, T-Cell,Receptors, CXCR4,RNA, Small Interfering,Signal Transduction,T-Lymphocytes |
| Related Products |
05-777 |
| Pub Med ID |
19426503 |
| |
|
TCR and CXCR4-mediated signaling appears to be reciprocally regulated pathways. TCR activation dampens the chemotactic response towards the CXCR4 ligand CXCL12, while T cells exposed to CXCL12 are less prone to subsequent TCR-activation. The heterotrimeric G proteins Galphaq and Galphai2 have been implicated in CXCR4-signaling and we have recently also reported the possible involvement of Galphaq in TCR-dependent activation of Lck (Ngai et al., Eur. J. Immunol., 2008, 38: 32083218). Here we examined the role of Galphaq in migration and TCR activation.
