• Carlo Bavassano, Letizia Marvaldi, Michiel Langeslag, Bettina Sarg, Herbert Lindner, Lars Klimaschewski, Michaela Kress, Antonio Ferrer-Montiel, and Hans-Günther Knaus.
• Division of Cellular and Molecular Pharmacology, Medical University Innsbruck, Peter-Mayr strasse 1, 6020 Innsbruck, Austria. Electronic address: carlo.bavassano@i-med.ac.at.
• Biochim. Biophys. Acta. 2013 Dec 1; 1833 (12): 3166-3175.

AbstractThe Transient Receptor Potential Vanilloid 1 (TRPV1, vanilloid receptor 1) ion channel plays a key role in the perception of thermal and inflammatory pain, however, its molecular environment in dorsal root ganglia (DRG) is largely unexplored. Utilizing a panel of sequence-directed antibodies against TRPV1 protein and mouse DRG membranes, the channel complex from mouse DRG was detergent-solubilized, isolated by immunoprecipitation and subsequently analyzed by mass spectrometry. A number of potential TRPV1 interaction partners were identified, among them cytoskeletal proteins, signal transduction molecules, and established ion channel subunits. Based on stringent specificity criteria, the voltage-gated K(+) channel beta 2 subunit (Kvβ2), an accessory subunit of voltage-gated K(+) channels, was identified of being associated with native TRPV1 channels. Reverse co-immunoprecipitation and antibody co-staining experiments confirmed TRPV1/Kvβ2 association. Biotinylation assays in the presence of Kvβ2 demonstrated increased cell surface expression levels of TRPV1, while patch-clamp experiments resulted in a significant increase of TRPV1 sensitivity to capsaicin. Our work shows, for the first time, the association of a Kvβ subunit with TRPV1 channels, and suggests that such interaction may play a role in TRPV1 channel trafficking to the plasma membrane. © 2013.

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