• Gene deletion studies revealed that membrane proteins stomatin and STOML3, as well as the acid‐sensing ion channels ASIC2 and ASIC3, regulate mechanosensory transduction. • Both stomatin and STOML3 interact with ASIC proteins and we asked if deletion of two interacting proteins has a more than additive effect on the mechanosensitivity of cutaneous sensory afferents. • A detailed electrophysiological comparison of sensory afferent phenotypes observed in asic3−/−:stomatin−/−, asic3−/−:stoml3−/− and asic2−/−:stomatin−/− mutant mice compared to their respective single gene mutants revealed especially strong effects on the mechanosensitivity of thinly myelinated mechanonociceptors in double mutants. • Deletion of the asic3 gene or pharmacological blockade of this channel decreased adaptation rates specifically in rapidly adapting mechanoreceptors, an effect not exacerbated by deletion of stomatin‐domain genes. • This study reveals that loss of stomatin–ASIC interactions can have profound effects on mechanosensitivity in specific subsets of skin afferents; interfering with such interactions could have potential for treating mechanical pain.
Stomatin-domain protein interactions with acid-sensing ion channels modulate nociceptor mechanosensitivity
R. Moshourab,Christiane Wetzel,C. Martínez-Salgado,G. Lewin
Published 2013 in Journal of Physiology
ABSTRACT
PUBLICATION RECORD
- Publication year
2013
- Venue
Journal of Physiology
- Publication date
2013-08-19
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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