The sigma receptor as a ligand-regulated auxiliary potassium channel subunit - PubMed (original) (raw)
The sigma receptor as a ligand-regulated auxiliary potassium channel subunit
Ebru Aydar et al. Neuron. 2002.
Free article
Abstract
The sigma receptor is a novel protein that mediates the modulation of ion channels by psychotropic drugs through a unique transduction mechanism depending neither on G proteins nor protein phosphorylation. The present study investigated sigma receptor signal transduction by reconstituting responses in Xenopus oocytes. Sigma receptors modulated voltage-gated K+ channels (Kv1.4 or Kv1.5) in different ways in the presence and absence of ligands. Association between Kv1.4 channels and sigma receptors was demonstrated by coimmunoprecipitation. These results indicate a novel mechanism of signal transduction dependent on protein-protein interactions. Domain accessibility experiments suggested a structure for the sigma receptor with two cytoplasmic termini and two membrane-spanning segments. The ligand-independent effects on channels suggest that sigma receptors serve as auxiliary subunits to voltage-gated K+ channels with distinct functional interactions, depending on the presence or absence of ligand.
Similar articles
- Membrane-delimited coupling between sigma receptors and K+ channels in rat neurohypophysial terminals requires neither G-protein nor ATP.
Lupardus PJ, Wilke RA, Aydar E, Palmer CP, Chen Y, Ruoho AE, Jackson MB. Lupardus PJ, et al. J Physiol. 2000 Aug 1;526 Pt 3(Pt 3):527-39. doi: 10.1111/j.1469-7793.2000.00527.x. J Physiol. 2000. PMID: 10922005 Free PMC article. - Phosphorylation-dependent and phosphorylation-independent modes of modulation of shaker family voltage-gated potassium channels by SRC family protein tyrosine kinases.
Nitabach MN, Llamas DA, Thompson IJ, Collins KA, Holmes TC. Nitabach MN, et al. J Neurosci. 2002 Sep 15;22(18):7913-22. doi: 10.1523/JNEUROSCI.22-18-07913.2002. J Neurosci. 2002. PMID: 12223544 Free PMC article. - Sigma receptor photolabeling and sigma receptor-mediated modulation of potassium channels in tumor cells.
Wilke RA, Mehta RP, Lupardus PJ, Chen Y, Ruoho AE, Jackson MB. Wilke RA, et al. J Biol Chem. 1999 Jun 25;274(26):18387-92. doi: 10.1074/jbc.274.26.18387. J Biol Chem. 1999. PMID: 10373444 - The pharmacology of sigma-1 receptors.
Maurice T, Su TP. Maurice T, et al. Pharmacol Ther. 2009 Nov;124(2):195-206. doi: 10.1016/j.pharmthera.2009.07.001. Epub 2009 Jul 18. Pharmacol Ther. 2009. PMID: 19619582 Free PMC article. Review. - 5-HT2 receptors-mediated modulation of voltage-gated K+ channels and neurophysiopathological correlates.
D'Adamo MC, Servettini I, Guglielmi L, Di Matteo V, Di Maio R, Di Giovanni G, Pessia M. D'Adamo MC, et al. Exp Brain Res. 2013 Oct;230(4):453-62. doi: 10.1007/s00221-013-3555-8. Epub 2013 May 24. Exp Brain Res. 2013. PMID: 23702970 Review.
Cited by
- Dynamic interaction between sigma-1 receptor and Kv1.2 shapes neuronal and behavioral responses to cocaine.
Kourrich S, Hayashi T, Chuang JY, Tsai SY, Su TP, Bonci A. Kourrich S, et al. Cell. 2013 Jan 17;152(1-2):236-47. doi: 10.1016/j.cell.2012.12.004. Cell. 2013. PMID: 23332758 Free PMC article. - The regulatory role of endoplasmic reticulum chaperone proteins in neurodevelopment.
Sun H, Wu M, Wang M, Zhang X, Zhu J. Sun H, et al. Front Neurosci. 2022 Nov 15;16:1032607. doi: 10.3389/fnins.2022.1032607. eCollection 2022. Front Neurosci. 2022. PMID: 36458041 Free PMC article. Review. - Ligand-dependent localization and intracellular stability of sigma-1 receptors in CHO-K1 cells.
Mavlyutov TA, Ruoho AE. Mavlyutov TA, et al. J Mol Signal. 2007 Sep 20;2:8. doi: 10.1186/1750-2187-2-8. J Mol Signal. 2007. PMID: 17883859 Free PMC article. - Non-canonical Targets Mediating the Action of Drugs of Abuse: Cocaine at the Sigma-1 Receptor as an Example.
Su TP. Su TP. Front Neurosci. 2019 Jul 23;13:761. doi: 10.3389/fnins.2019.00761. eCollection 2019. Front Neurosci. 2019. PMID: 31396041 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases