Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-6-28
pubmed:databankReference
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha Subunits, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha..., http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha..., http://linkedlifedata.com/resource/pubmed/chemical/Glycine, http://linkedlifedata.com/resource/pubmed/chemical/Gnat1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transducin, http://linkedlifedata.com/resource/pubmed/chemical/UNC119 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/odr-3 protein, C elegans
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1546-1726
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
874-80
pubmed:dateRevised
2011-9-30
pubmed:meshHeading
pubmed-meshheading:21642972-Adaptor Proteins, Signal Transducing, pubmed-meshheading:21642972-Animals, pubmed-meshheading:21642972-Animals, Genetically Modified, pubmed-meshheading:21642972-Caenorhabditis elegans, pubmed-meshheading:21642972-Caenorhabditis elegans Proteins, pubmed-meshheading:21642972-Cattle, pubmed-meshheading:21642972-Dark Adaptation, pubmed-meshheading:21642972-GTP Phosphohydrolases, pubmed-meshheading:21642972-GTP-Binding Protein alpha Subunits, pubmed-meshheading:21642972-GTP-Binding Protein alpha Subunits, G12-G13, pubmed-meshheading:21642972-GTP-Binding Protein alpha Subunits, Gi-Go, pubmed-meshheading:21642972-Gene Expression Regulation, pubmed-meshheading:21642972-Glycine, pubmed-meshheading:21642972-Green Fluorescent Proteins, pubmed-meshheading:21642972-Humans, pubmed-meshheading:21642972-Mice, pubmed-meshheading:21642972-Mice, Knockout, pubmed-meshheading:21642972-Models, Chemical, pubmed-meshheading:21642972-Models, Molecular, pubmed-meshheading:21642972-Mutation, pubmed-meshheading:21642972-Protein Binding, pubmed-meshheading:21642972-Protein Structure, Quaternary, pubmed-meshheading:21642972-Protein Transport, pubmed-meshheading:21642972-Sensory Receptor Cells, pubmed-meshheading:21642972-Signal Transduction, pubmed-meshheading:21642972-Time Factors, pubmed-meshheading:21642972-Transducin
pubmed:year
2011
pubmed:articleTitle
UNC119 is required for G protein trafficking in sensory neurons.
pubmed:affiliation
Department of Ophthalmology, University of Utah Health Science Center, Salt Lake City, Utah, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural