| First Author | Wu YC | Year | 2013 |
| Journal | Biochim Biophys Acta | Volume | 1833 |
| Issue | 12 | Pages | 3145-3154 |
| PubMed ID | 23994616 | Mgi Jnum | J:277872 |
| Mgi Id | MGI:6355742 | Doi | 10.1016/j.bbamcr.2013.08.009 |
| Citation | Wu YC, et al. (2013) A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling of the A2A adenosine receptor. Biochim Biophys Acta 1833(12):3145-3154 |
| abstractText | The A2A adenosine receptor (A2AR) is a G-protein-coupled receptor that contains a long cytoplasmic carboxyl terminus (A2AR-C). We report here that Gas-2 like 2 (G2L2) is a new interacting partner of A2AR-C. The interaction between A2AR and G2L2 was verified by GST pull-down, co-immunoprecipitation, immunocytochemical staining, and fluorescence resonance energy transfer. Expression of G2L2 increased the intracellular cAMP content evoked by A2AR in an A2AR-C-dependent manner. Immunoprecipitation and pull-down assays demonstrated that G2L2 selectively bound to A2AR-C and the inactive form of Galphas to facilitate the recruitment of the trimeric G protein complex to the proximal position of A2AR for efficient activation. Collectively, G2L2 is a new effector that controls the action of A2AR by modulating its ability to regulate the Galphas-mediated cAMP contents. |
