| Literature DB >> 21642972 |
Houbin Zhang1, Ryan Constantine, Sergey Vorobiev, Yang Chen, Jayaraman Seetharaman, Yuanpeng Janet Huang, Rong Xiao, Gaetano T Montelione, Cecilia D Gerstner, M Wayne Davis, George Inana, Frank G Whitby, Erik M Jorgensen, Christopher P Hill, Liang Tong, Wolfgang Baehr.
Abstract
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 acylated Tα N-terminal peptide at 2.0 Å revealed that the lipid chain is buried deeply into UNC119's hydrophobic cavity. UNC119 bound Tα-GTP, inhibiting its GTPase activity, thereby providing a stable UNC119-Tα-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 Gα subunit cofactor essential for G protein trafficking in sensory cilia.Entities:
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Year: 2011 PMID： 21642972 PMCID： PMC3178889 DOI： 10.1038/nn.2835
Source DB: PubMed Journal: Nat Neurosci ISSN： 1097-6256 Impact factor: 24.884