| First Author | Zhang H | Year | 2011 |
| Journal | Nat Neurosci | Volume | 14 |
| Issue | 7 | Pages | 874-80 |
| PubMed ID | 21642972 | Mgi Jnum | J:174011 |
| Mgi Id | MGI:5050777 | Doi | 10.1038/nn.2835 |
| Citation | Zhang H, et al. (2011) UNC119 is required for G protein trafficking in sensory neurons. Nat Neurosci 14(7):874-80 |
| abstractText | UNC119 is widely expressed among vertebrates and other phyla. We found that UNC119 recognized the acylated N terminus of the rod photoreceptor transducin alpha (Talpha) subunit and Caenorhabditis elegans G proteins ODR-3 and GPA-13. The crystal structure of human UNC119 at 1.95-A resolution revealed an immunoglobulin-like beta-sandwich fold. Pulldowns and isothermal titration calorimetry revealed a tight interaction between UNC119 and acylated Galpha peptides. The structure of co-crystals of UNC119 with an acylated Talpha N-terminal peptide at 2.0 A revealed that the lipid chain is buried deeply into UNC119's hydrophobic cavity. UNC119 bound Talpha-GTP, inhibiting its GTPase activity, thereby providing a stable UNC119-Talpha-GTP complex capable of diffusing from the inner segment back to the outer segment after light-induced translocation. UNC119 deletion in both mouse and C. elegans led to G protein mislocalization. Thus, UNC119 is a Galpha subunit cofactor essential for G protein trafficking in sensory cilia. |
