Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-1-26
pubmed:abstractText
Several recent studies have shown that neuroligin 2 (NL2), a component of the cell adhesion neurexins-neuroligins complex, is localized postsynaptically at hippocampal and other inhibitory synapses throughout the brain. Other studies have shown that components of the dystroglycan complex are also localized at a subset of inhibitory synapses and are coexpressed with NL2 in brain. These data prompted us to undertake a comparative study between the localization of NL2 and the dystroglycan complex in the rodent retina. First, we determined that NL2 mRNA is expressed both in the inner and in the outer nuclear layers. Second, we found that NL2 is localized both in the inner and in the outer synaptic plexiform layers. In the latter, the horseshoe-shaped pattern of NL2 and its extensive colocalization with RIM2, a component of the presynaptic active zone at ribbon synapses, argue that NL2 is localized presynaptically at photoreceptor terminals. Third, comparison of NL2 and the dystroglycan complex distribution patterns reveals that, despite their coexpression in the outer plexiform layer, they are spatially segregated within distinct domains of the photoreceptor terminals, where NL2 is selectively associated with the active zone and the dystroglycan complex is distally distributed in the lateral regions. Finally, we report that the dystroglycan deficiency in the mdx(3cv) mouse does not alter NL2 localization in the outer plexiform layer. These data show that the NL2- and dystroglycan-containing complexes are differentially localized in the presynaptic photoreceptor terminals and suggest that they may serve distinct functions in retina.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal, http://linkedlifedata.com/resource/pubmed/chemical/Dlgh4 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Dystroglycans, http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Rim2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Synaptophysin, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Glutamate Transport..., http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Inhibitory Amino Acid..., http://linkedlifedata.com/resource/pubmed/chemical/Viaat protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/neuroligin 2, http://linkedlifedata.com/resource/pubmed/chemical/rab3 GTP-Binding Proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1097-4547
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
837-49
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:19859968-Animals, pubmed-meshheading:19859968-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:19859968-Cells, Cultured, pubmed-meshheading:19859968-Cerebral Cortex, pubmed-meshheading:19859968-Dystroglycans, pubmed-meshheading:19859968-Embryo, Mammalian, pubmed-meshheading:19859968-Guanylate Kinase, pubmed-meshheading:19859968-Hippocampus, pubmed-meshheading:19859968-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:19859968-Membrane Proteins, pubmed-meshheading:19859968-Mice, pubmed-meshheading:19859968-Mice, Inbred mdx, pubmed-meshheading:19859968-Nerve Tissue Proteins, pubmed-meshheading:19859968-Neurons, pubmed-meshheading:19859968-Rats, pubmed-meshheading:19859968-Rats, Sprague-Dawley, pubmed-meshheading:19859968-Retina, pubmed-meshheading:19859968-Synapses, pubmed-meshheading:19859968-Synaptophysin, pubmed-meshheading:19859968-Vesicular Glutamate Transport Protein 1, pubmed-meshheading:19859968-Vesicular Inhibitory Amino Acid Transport Proteins, pubmed-meshheading:19859968-rab3 GTP-Binding Proteins
pubmed:year
2010
pubmed:articleTitle
Synaptic localization of neuroligin 2 in the rodent retina: comparative study with the dystroglycan-containing complex.
pubmed:affiliation
Department of Cellular and Physiological Sciences, Life Sciences Institute, The University of British Columbia, Vancouver, British Columbia, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't