Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2008-7-14
pubmed:abstractText
Arl2 and Arl3, members of the Arf subfamily of small G proteins, are believed to be involved in ciliary and microtubule-dependent processes. Recently, we could identify RP2, responsible for a variant of X-linked retinitis pigmentosa, as the Arl3-specific GAP. Here, we have characterized Arl2/3 interactions. We show the formation of a ternary complex between Arl3, its cognate GAP RP2 and its retinal effector HRG4. This complex seems to be important for photoreceptor function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors, http://linkedlifedata.com/resource/pubmed/chemical/ARL2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/ARL3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic Nucleotide..., http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PDE6D protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RP2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/UNC119 protein, human
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
582
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2501-7
pubmed:dateRevised
2010-10-8
pubmed:meshHeading
pubmed-meshheading:18588884-ADP-Ribosylation Factors, pubmed-meshheading:18588884-Adaptor Proteins, Signal Transducing, pubmed-meshheading:18588884-Amino Acid Sequence, pubmed-meshheading:18588884-Cyclic Nucleotide Phosphodiesterases, Type 6, pubmed-meshheading:18588884-Eye Proteins, pubmed-meshheading:18588884-GTP-Binding Proteins, pubmed-meshheading:18588884-GTPase-Activating Proteins, pubmed-meshheading:18588884-Guanosine Diphosphate, pubmed-meshheading:18588884-Humans, pubmed-meshheading:18588884-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:18588884-Membrane Proteins, pubmed-meshheading:18588884-Molecular Sequence Data, pubmed-meshheading:18588884-Photoreceptor Cells, Vertebrate, pubmed-meshheading:18588884-Protein Conformation, pubmed-meshheading:18588884-Signal Transduction
pubmed:year
2008
pubmed:articleTitle
Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex.
pubmed:affiliation
Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, Dortmund, Germany.
pubmed:publicationType
Journal Article