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• W2023272294 startingPage "435" @default.
• W2023272294 abstract "Inhibitory glycine receptors (GlyRs) are densely packed in the postsynaptic membrane due to a high-affinity interaction of their β-subunits with the scaffolding protein gephyrin. Here, we used an affinity-based proteomic approach to identify the trafficking proteins Vacuolar Protein Sorting 35 (Vps35) and Neurobeachin (Nbea) as novel GlyR β-subunit (GlyRβ) interacting proteins in rat brain. Recombinant Vps35 and a central fragment of Nbea bound to the large intracellular loop of GlyRβ in glutathione-S-transferase pull-downs; in addition, Vps35 displayed binding to gephyrin. Immunocytochemical staining of spinal cord sections revealed Nbea immunoreactivity apposed to and colocalizing with marker proteins of inhibitory synapses. Our data are consistent with roles of Vps35 and Nbea in the retrieval and post-Golgi trafficking of synaptic GlyRs and possibly other neurotransmitter receptors." @default.
• W2023272294 created "2016-06-24" @default.
• W2023272294 creator A5029063039 @default.
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• W2023272294 creator A5061687655 @default.
• W2023272294 creator A5070853048 @default.
• W2023272294 creator A5091096048 @default.
• W2023272294 date "2011-09-01" @default.
• W2023272294 modified "2023-09-26" @default.
• W2023272294 title "The trafficking proteins Vacuolar Protein Sorting 35 and Neurobeachin interact with the glycine receptor β-subunit" @default.
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• W2023272294 doi "https://doi.org/10.1016/j.bbrc.2011.07.110" @default.
• W2023272294 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21821005" @default.
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