The Present address of M. Dreger is University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK.
Identification and characterization of a Ca2+-sensitive interaction of the vanilloid receptor TRPV1 with tubulin
Article first published online: 18 NOV 2004
Journal of Neurochemistry
Volume 91, Issue 5, pages 1092–1103, December 2004
How to Cite
Goswami, C., Dreger, M., Jahnel, R., Bogen, O., Gillen, C. and Hucho, F. (2004), Identification and characterization of a Ca2+-sensitive interaction of the vanilloid receptor TRPV1 with tubulin. Journal of Neurochemistry, 91: 1092–1103. doi: 10.1111/j.1471-4159.2004.02795.x
- Issue published online: 18 NOV 2004
- Article first published online: 18 NOV 2004
- Resubmitted manuscript received July 21, 2004; accepted July 23, 2004.
- calcium dependence;
- capsaicin receptor;
- cytoskeleton interaction;
- transient receptor potential V1
The vanilloid receptor TRPV1 plays a well-established functional role in the detection of a range of chemical and thermal noxious stimuli, such as those associated with tissue inflammation and the resulting pain. TRPV1 activation results in membrane depolarization, but may also trigger intracellular Ca2+-signalling events. In a proteomic screen for proteins associated with the C-terminal sequence of TRPV1, we identified β-tubulin as a specific TRPV1-interacting protein. We demonstrate that the TRPV1 C-terminal tail is capable of binding tubulin dimers, as well as of binding polymerized microtubules. The interaction is Ca2+-sensitive, and affects microtubule properties, such as microtubule sensitivity towards low temperatures and nocodazole. Our data thus provide compelling evidence for the interaction of TRPV1 with the cytoskeleton. The Ca2+-sensitivity of this interaction suggests that the microtubule cytoskeleton at the cell membrane may be a downstream effector of TRPV1 activation.