Identification and characterization of a Ca2+‐sensitive interaction of the vanilloid receptor TRPV1 with tubulin

• Published in: Journal of neurochemistry Vol. 91; no. 5; pp. 1092 - 1103
• Main Authors: Goswami, C., Dreger, M., Jahnel, R., Bogen, O., Gillen, C., Hucho, F.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Science Ltd 01-12-2004; Blackwell
• Subjects: Animals; Biological and medical sciences; Blotting, Western - methods; Calcium - metabolism; calcium dependence; Calcium Signaling - physiology; capsaicin receptor; Carrier Proteins - metabolism; Cell Line; Cell receptors; Cell structures and functions; cytoskeleton interaction; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Immunohistochemistry - methods; Immunoprecipitation - methods; Ion Channels - genetics; Ion Channels - metabolism; Maltose-Binding Proteins; Miscellaneous; Models, Biological; Molecular and cellular biology; Phalloidine - metabolism; Protein Binding; Protein Structure, Tertiary; Proteomics - methods; Rats; Recombinant Proteins - metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods; Spinal Cord - metabolism; Swine; Temperature; Transfection - methods; transient receptor potential V1; TRPV Cation Channels; Tubulin - metabolism; Noxious stimulus; capsaicin receptor; Calcium; calcium dependence; Inflammation; Protein; Characterization; Depolarization; transient receptor potential V1; Sensitivity; TRPV1 vanilloid receptor; Pain; Tubulin; Proteomics; cytoskeleton interaction; Intracellular; Microtubule
• ISSN: 0022-3042; 1471-4159
• DOI: 10.1111/j.1471-4159.2004.02795.x

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.