Unknown

Dataset Information

0

UNC119 is required for G protein trafficking in sensory neurons.


ABSTRACT: UNC119 is widely expressed among vertebrates and other phyla. We found that UNC119 recognized the acylated N terminus of the rod photoreceptor transducin ? (T?) subunit and Caenorhabditis elegans G proteins ODR-3 and GPA-13. The crystal structure of human UNC119 at 1.95-Å resolution revealed an immunoglobulin-like ?-sandwich fold. Pulldowns and isothermal titration calorimetry revealed a tight interaction between UNC119 and acylated G? peptides. The structure of co-crystals of UNC119 with an acylated T? N-terminal peptide at 2.0 Å revealed that the lipid chain is buried deeply into UNC119's hydrophobic cavity. UNC119 bound T?-GTP, inhibiting its GTPase activity, thereby providing a stable UNC119-T?-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 G? subunit cofactor essential for G protein trafficking in sensory cilia.

SUBMITTER: Zhang H 

PROVIDER: S-EPMC3178889 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications


UNC119 is widely expressed among vertebrates and other phyla. We found that UNC119 recognized the acylated N terminus of the rod photoreceptor transducin α (Tα) subunit and Caenorhabditis elegans G proteins ODR-3 and GPA-13. The crystal structure of human UNC119 at 1.95-Å resolution revealed an immunoglobulin-like β-sandwich fold. Pulldowns and isothermal titration calorimetry revealed a tight interaction between UNC119 and acylated Gα peptides. The structure of co-crystals of UNC119 with an acy  ...[more]

Similar Datasets

| S-EPMC6191072 | biostudies-literature
| S-EPMC423267 | biostudies-literature
| S-EPMC3190703 | biostudies-literature
| S-EPMC6360273 | biostudies-literature
| S-EPMC19204 | biostudies-literature
| S-EPMC6314548 | biostudies-literature
| S-EPMC6973269 | biostudies-literature
| S-EPMC6218061 | biostudies-literature
| S-EPMC7706712 | biostudies-literature
| S-EPMC4390579 | biostudies-literature