Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

Subunit-specific inhibition of acid sensing ion channels by stomatin-like protein 1

[thumbnail of Article] PDF (Article) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
2MB
[thumbnail of Supplemental Material] PDF (Supplemental Material) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
485kB

Item Type:Article
Title:Subunit-specific inhibition of acid sensing ion channels by stomatin-like protein 1
Creators Name:Kozlenkov, A., Lapatsina, L., Lewin, G.R. and Smith, E.S.J.
Abstract:There are five mammalian stomatin-domain genes all of which encode peripheral membrane proteins that can modulate ion channel function. Here we examined the ability of stomatin-like protein 1 (STOML1) to modulate the proton-sensitive members of the acid-sensing ion channel (ASIC) family. We find that STOML1 profoundly inhibits ASIC1a, but has no effect on the splice variant ASIC1b. The inactivation time constant of ASIC3 is also accelerated by STOML1. We examined STOML1 null mutant mice with a beta-galactosidase-neomycin cassette gene-trap reporter driven from the STOML1 gene locus, which indicated that STOML1 is expressed in at least 50% of dorsal root ganglion (DRG) neurones. Patch clamp recordings from mouse DRG neurones identified a trend for larger proton-gated currents in neurones lacking STOML1, which was due to a contribution of effects upon both transient and sustained currents, at different pH values, a finding consistent with an endogenous inhibitory function for STOML1.
Keywords:Electrophysiology, Ion Channel Modulation, Sensory Nurons, Animals, Mice
Source:Journal of Physiology
ISSN:0022-3751
Publisher:Wiley-Blackwell
Volume:592
Number:Pt 4
Page Range:557-569
Date:15 February 2014
Official Publication:https://doi.org/10.1113/jphysiol.2013.258657
PubMed:View item in PubMed

Repository Staff Only: item control page

Downloads

Downloads per month over past year

Open Access
MDC Library