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  AMPA Receptors Commandeer an Ancient Cargo Exporter for Use as an Auxiliary Subunit for Signaling

Harmel, N., Cokic, B., Zolles, G., Berkefeld, H., Mauric, V., Fakler, B., et al. (2012). AMPA Receptors Commandeer an Ancient Cargo Exporter for Use as an Auxiliary Subunit for Signaling. PLOS ONE, 7(1): e30681, pp. [1]-[9]. doi:10.1371/journal.pone.0030681.

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 Creators:
Harmel, Nadine1, Author
Cokic, Barbara2, Author           
Zolles, Gerd1, Author
Berkefeld, Henrike1, Author
Mauric, Veronika1, Author
Fakler, Bernd1, Author
Stein, Valentin1, Author
Kloecker, Nikolaj1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Max Planck Research Group: Synaptic Receptor Trafficking / Stein, MPI of Neurobiology, Max Planck Society, ou_1113557              

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Free keywords: LONG-TERM POTENTIATION; ENDOPLASMIC-RETICULUM; ER EXPORT; SYNAPTIC PLASTICITY; KINETIC-PROPERTIES; GLUTAMATE RECEPTORS; CORNICHON PROTEINS; LENTIVIRAL VECTORS; TRAFFICKING; CHANNELSBiology;
 Abstract: Fast excitatory neurotransmission in the mammalian central nervous system is mainly mediated by ionotropic glutamate receptors of the AMPA subtype (AMPARs). AMPARs are protein complexes of the pore-lining alpha-subunits GluA1-4 and auxiliary beta-subunits modulating their trafficking and gating. By a proteomic approach, two homologues of the cargo exporter cornichon, CNIH-2 and CNIH-3, have recently been identified as constituents of native AMPARs in mammalian brain. In heterologous reconstitution experiments, CNIH-2 promotes surface expression of GluAs and modulates their biophysical properties. However, its relevance in native AMPAR physiology remains controversial. Here, we have studied the role of CNIH-2 in GluA processing both in heterologous cells and primary rat neurons. Our data demonstrate that CNIH-2 serves an evolutionarily conserved role as a cargo exporter from the endoplasmic reticulum (ER). CNIH-2 cycles continuously between ER and Golgi complex to pick up cargo protein in the ER and then to mediate its preferential export in a coat protein complex (COP) II dependent manner. Interaction with GluA subunits breaks with this ancestral role of CNIH-2 confined to the early secretory pathway. While still taking advantage of being exported preferentially from the ER, GluAs recruit CNIH-2 to the cell surface. Thus, mammalian AMPARs commandeer CNIH-2 for use as a bona fide auxiliary subunit that is able to modify receptor signaling.

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Language(s): eng - English
 Dates: 2012
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
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Title: PLOS ONE
Source Genre: Journal
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Publ. Info: 185 BERRY ST, STE 1300, SAN FRANCISCO, CA 94107 USA : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 7 (1) Sequence Number: e30681 Start / End Page: [1] - [9] Identifier: ISSN: 1932-6203