Literature DB >> 14723974

Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts.

Jeffrey R Martens1, Kristen O'Connell, Michael Tamkun.   

Abstract

Voltage-gated K(+) channels are an important determinant of cellular excitability and key components of multiple signal transduction pathways. However, relatively little is known about the mechanisms of K(V) channel localization or their membrane partitioning. Lipid rafts are specialized membrane microdomains that are rich in sphingolipids and cholesterol. These rafts have been implicated in the organization of many membrane-associated signaling pathways and are currently the focus of intense interest in the scientific community. Biochemical and functional evidence indicate that K(V) channels, in addition to other ion channels, localize to lipid raft microdomains on the cell surface. Although several important questions regarding specific mechanisms of channel localization remain, emerging data indicate that protein-lipid interactions should be considered as a new mechanism of ion channel localization and compartmentation that might permit the therapeutic modulation of channel properties via alteration in membrane lipids.

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Year:  2004        PMID: 14723974     DOI: 10.1016/j.tips.2003.11.007

Source DB:  PubMed          Journal:  Trends Pharmacol Sci        ISSN: 0165-6147            Impact factor:   14.819


  66 in total

Review 1.  The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology.

Authors:  Rennolds S Ostrom; Paul A Insel
Journal:  Br J Pharmacol       Date:  2004-08-02       Impact factor: 8.739

2.  Transbilayer peptide sorting between raft and nonraft bilayers: comparisons of detergent extraction and confocal microscopy.

Authors:  Adriana Vidal; Thomas J McIntosh
Journal:  Biophys J       Date:  2005-05-20       Impact factor: 4.033

Review 3.  How proteins come together in the plasma membrane and function in macromolecular assemblies: focus on receptor mosaics.

Authors:  Luigi F Agnati; Diego Guidolin; Susanna Genedani; Sergi Ferré; Albertino Bigiani; Amina S Woods; Kjell Fuxe
Journal:  J Mol Neurosci       Date:  2005       Impact factor: 3.444

4.  Kv1.5 association modifies Kv1.3 traffic and membrane localization.

Authors:  Rubén Vicente; Núria Villalonga; Maria Calvo; Artur Escalada; Carles Solsona; Concepció Soler; Michael M Tamkun; Antonio Felipe
Journal:  J Biol Chem       Date:  2008-01-24       Impact factor: 5.157

5.  Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors.

Authors:  Parthena D Sanxaridis; Michelle A Cronin; Satinder S Rawat; Girma Waro; Usha Acharya; Susan Tsunoda
Journal:  Mol Cell Neurosci       Date:  2007-06-27       Impact factor: 4.314

Review 6.  Bioelectric mechanisms in regeneration: Unique aspects and future perspectives.

Authors:  Michael Levin
Journal:  Semin Cell Dev Biol       Date:  2009-05-03       Impact factor: 7.727

7.  The role of cell cholesterol and the cytoskeleton in the interaction between IK1 and maxi-K channels.

Authors:  Victor G Romanenko; Kurt S Roser; James E Melvin; Ted Begenisich
Journal:  Am J Physiol Cell Physiol       Date:  2009-01-28       Impact factor: 4.249

8.  Lipid raft segregation modulates TRPM8 channel activity.

Authors:  Cruz Morenilla-Palao; María Pertusa; Víctor Meseguer; Hugo Cabedo; Félix Viana
Journal:  J Biol Chem       Date:  2009-01-27       Impact factor: 5.157

9.  Multiple Kv1.5 targeting to membrane surface microdomains.

Authors:  Ramón Martínez-Mármol; Núria Villalonga; Laura Solé; Rubén Vicente; Michael M Tamkun; Concepció Soler; Antonio Felipe
Journal:  J Cell Physiol       Date:  2008-12       Impact factor: 6.384

10.  Implications of Human Transient Receptor Potential Melastatin 8 (TRPM8) Channel Gating from Menthol Binding Studies of the Sensing Domain.

Authors:  Parthasarathi Rath; Jacob K Hilton; Nicholas J Sisco; Wade D Van Horn
Journal:  Biochemistry       Date:  2015-12-23       Impact factor: 3.162

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