ASICs (acid-sensing ion channels) are H+-gated Na+ channels with a widespread expression pattern in the central and the peripheral nervous system. ASICs have a simple topology with two transmembrane domains, cytoplasmic termini and a large ectodomain between the transmembrane domains; this topology has been confirmed by the crystal structure of chicken ASIC1. ASIC1a and ASIC1b are two variants encoded by the asic1 gene. The variable part of the protein includes the cytoplasmic N-terminus, the first transmembrane domain and approximately the first third of the ectodomain. Both variants contain two consensus sequences for N-linked glycosylation in the common, distal part of the ectodomain. In contrast with ASIC1a, ASIC1b contains two additional consensus sequences in the variable, proximal part of the ectodomain. Here we show that all the extracellular asparagine residues within the putative consensus sequences for N-glycosylation carry glycans. The two common distal glycans increase surface expression of the channels, but are no absolute requirement for channel activity. In sharp contrast, the presence of at least one of the two proximal glycans, which are specific to ASIC1b, is an absolute requirement for surface expression of ASIC1b. This result suggests substantial differences in the structure of the proximal ectodomain between the two ASIC1 variants.
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Research Article|
May 28 2008
Differential effects of N-glycans on surface expression suggest structural differences between the acid-sensing ion channel (ASIC) 1a and ASIC1b
Ivan Kadurin;
Ivan Kadurin
*Institute of Physiology II, University of Würzburg, Röntgenring 9, D-97070 Würzburg, Germany
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Andjelko Golubovic;
Andjelko Golubovic
*Institute of Physiology II, University of Würzburg, Röntgenring 9, D-97070 Würzburg, Germany
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Lilia Leisle;
Lilia Leisle
1
*Institute of Physiology II, University of Würzburg, Röntgenring 9, D-97070 Würzburg, Germany
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Hermann Schindelin;
Hermann Schindelin
†Rudolf Virchow Center for Experimental Biomedicine and Institute of Structural Biology, University of Würzburg, Versbacher Strasse 9, D-97078 Würzburg, Germany
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Stefan Gründer
Stefan Gründer
2
*Institute of Physiology II, University of Würzburg, Röntgenring 9, D-97070 Würzburg, Germany
2To whom correspondence should be sent at the present address: Institute of Physiology, RWTH Aachen University, Pauwelsstr. 30, D-52074 Aachen, Germany (email sgruender@ukaachen.de).
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Publisher: Portland Press Ltd
Received:
November 28 2007
Revision Received:
February 13 2008
Accepted:
February 29 2008
Accepted Manuscript online:
February 29 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem J (2008) 412 (3): 469–475.
Article history
Received:
November 28 2007
Revision Received:
February 13 2008
Accepted:
February 29 2008
Accepted Manuscript online:
February 29 2008
Citation
Ivan Kadurin, Andjelko Golubovic, Lilia Leisle, Hermann Schindelin, Stefan Gründer; Differential effects of N-glycans on surface expression suggest structural differences between the acid-sensing ion channel (ASIC) 1a and ASIC1b. Biochem J 15 June 2008; 412 (3): 469–475. doi: https://doi.org/10.1042/BJ20071614
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