Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2011-3-1
pubmed:abstractText
SynArfGEF, also known as BRAG3 or IQSEC3, is a member of the brefeldin A-resistant Arf-GEF/IQSEC family and was originally identified by screening for mRNA species associated with the post-synaptic density fraction. In this study, we demonstrate that synArfGEF activates Arf6, using Arf pull down and transferrin incorporation assays. Immunohistochemical analysis reveals that synArfGEF is present in somata and dendrites as puncta in close association with inhibitory synapses, whereas immunoelectron microscopic analysis reveals that synArfGEF localizes preferentially at post-synaptic specializations of symmetric synapses. Using yeast two-hybrid and pull down assays, we show that synArfGEF is able to bind utrophin/dystrophin and S-SCAM/MAGI-2 scaffolding proteins that localize at inhibitory synapses. Double immunostaining reveals that synArfGEF co-localizes with dystrophin and S-SCAM in cultured hippocampal neurons and cerebellar cortex, respectively. Both ?-dystroglycan and S-SCAM were immunoprecipitated from brain lysates using anti-synArfGEF IgG. Taken together, these findings suggest that synArfGEF functions as a novel regulator of Arf6 at inhibitory synapses and associates with the dystrophin-associated glycoprotein complex and S-SCAM.
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/ADP-ribosylation factor 6, http://linkedlifedata.com/resource/pubmed/chemical/Acvrinp1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/MAGI2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Magi2 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Inhibitory Amino Acid..., http://linkedlifedata.com/resource/pubmed/chemical/Viaat protein, mouse
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1471-4159
pubmed:author
pubmed:copyrightInfo
© 2011 The Authors. Journal of Neurochemistry © 2011 International Society for Neurochemistry.
pubmed:issnType
Electronic
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1122-37
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:21198641-ADP-Ribosylation Factors, pubmed-meshheading:21198641-Adaptor Proteins, Signal Transducing, pubmed-meshheading:21198641-Animals, pubmed-meshheading:21198641-Brain, pubmed-meshheading:21198641-Carrier Proteins, pubmed-meshheading:21198641-Cell Line, Transformed, pubmed-meshheading:21198641-Cercopithecus aethiops, pubmed-meshheading:21198641-Dystrophin, pubmed-meshheading:21198641-Gene Expression Regulation, pubmed-meshheading:21198641-Guanine Nucleotide Exchange Factors, pubmed-meshheading:21198641-Guanosine Triphosphate, pubmed-meshheading:21198641-Guanylate Kinase, pubmed-meshheading:21198641-Humans, pubmed-meshheading:21198641-Immunoprecipitation, pubmed-meshheading:21198641-Mice, pubmed-meshheading:21198641-Neurons, pubmed-meshheading:21198641-Protein Binding, pubmed-meshheading:21198641-Proteins, pubmed-meshheading:21198641-Synapses, pubmed-meshheading:21198641-Transfection, pubmed-meshheading:21198641-Two-Hybrid System Techniques, pubmed-meshheading:21198641-Vesicular Inhibitory Amino Acid Transport Proteins
pubmed:year
2011
pubmed:articleTitle
SynArfGEF is a guanine nucleotide exchange factor for Arf6 and localizes preferentially at post-synaptic specializations of inhibitory synapses.
pubmed:affiliation
Department of Anatomy, Kitasato University School of Medicine, Sagamihara, Kanagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't