| First Author | Bavassano C | Year | 2013 |
| Journal | Biochim Biophys Acta | Volume | 1833 |
| Issue | 12 | Pages | 3166-3175 |
| PubMed ID | 24036102 | Mgi Jnum | J:204072 |
| Mgi Id | MGI:5529556 | Doi | 10.1016/j.bbamcr.2013.09.001 |
| Citation | Bavassano C, et al. (2013) Identification of voltage-gated K(+) channel beta 2 (Kvbeta2) subunit as a novel interaction partner of the pain transducer Transient Receptor Potential Vanilloid 1 channel (TRPV1). Biochim Biophys Acta 1833(12):3166-75 |
| abstractText | The 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 (Kvbeta2), 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/Kvbeta2 association. Biotinylation assays in the presence of Kvbeta2 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 Kvbeta subunit with TRPV1 channels, and suggests that such interaction may play a role in TRPV1 channel trafficking to the plasma membrane. |
