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The trafficking proteins Vacuolar Protein Sorting 35 and Neurobeachin interact with the glycine receptor β-subunit

AuthorsPino, Isabel del; Paarmann, Ingo; Karas, Michael; Kilimann, Manfred W.; Betz, Heinrich
Glycine receptor
Retromer complex
Spinal cord
Vacuolar Protein Sorting 35
Issue DateSep-2011
PublisherAcademic Press
CitationBiochemical and Biophysical Research Communications 412(3): 435-440 (2011)
AbstractInhibitory 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.
Description6 p., 4 figures and references.
Publisher version (URL)http://dx.doi.org/10.1016/j.bbrc.2011.07.110
Appears in Collections:(IN) Artículos
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