ArticleScientific reports2016
Acid-Sensing Ion Channel 2a (ASIC2a) Promotes Surface Trafficking of ASIC2b via Heteromeric Assembly.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Molecular and biophysical features of hippocampal "lipid rafts aging" are modified by dietary n-3 long-chain polyunsaturated fatty acids.Aging cell · 2023Article
- Investigating role of ASIC2 in synaptic and behavioral responses to drugs of abuse.Frontiers in molecular biosciences · 2023Article
- Acid-Sensing Ion Channels and Mechanosensation.International journal of molecular sciences · 2021Review
- Cell-Type-Specific Expression Pattern of Proton-Sensing Receptors and Channels in Pituitary Gland.Biophysical journal · 2020Article
- Rapid resensitization of ASIC2a is conferred by three amino acid residues in the N terminus.The Journal of general physiology · 2019Article
- Targeted Acid-Sensing Ion Channel Therapies for Migraine.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2018Review
- Naked mole-rat acid-sensing ion channel 3 forms nonfunctional homomers, but functional heteromers.The Journal of biological chemistry · 2018Article
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Authors and funding
5 authors.
Funding
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Abstract
Acid-sensing ion channels (ASICs) are proton-activated cation channels that play important roles as typical proton sensors during pathophysiological conditions and normal synaptic activities. Among the ASIC subunits, ASIC2a and ASIC2b are alternative splicing products from the same gene, ACCN1. It has been shown that ASIC2 isoforms have differential subcellular distribution: ASIC2a targets the cell surface by itself, while ASIC2b resides in the ER. However, the underlying mechanism for this differential subcellular localization remained to be further elucidated. By constructing ASIC2 chimeras, we found that the first transmembrane (TM1) domain and the proximal post-TM1 domain (17 amino acids) of ASIC2a are critical for membrane targeting of the proteins. We also observed that replacement of corresponding residues in ASIC2b by those of ASIC2a conferred proton-sensitivity as well as surface expression to ASIC2b. We finally confirmed that ASIC2b is delivered to the cell surface from the ER by forming heteromers with ASIC2a, and that the N-terminal region of ASIC2a is additionally required for the ASIC2a-dependent membrane targeting of ASIC2b. Together, our study supports an important role of ASIC2a in membrane targeting of ASIC2b.
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