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Identification and characterization of a Ca 2+ ‐sensitive interaction of the vanilloid receptor TRPV1 with tubulin
Author(s) -
Goswami C.,
Dreger M.,
Jahnel R.,
Bogen O.,
Gillen C.,
Hucho F.
Publication year - 2004
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02795.x
Subject(s) - microtubule , trpv1 , nocodazole , microbiology and biotechnology , tubulin , chemistry , cytoskeleton , intracellular , biophysics , biochemistry , biology , receptor , cell , transient receptor potential channel
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 Ca 2+ ‐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 Ca 2+ ‐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 Ca 2+ ‐sensitivity of this interaction suggests that the microtubule cytoskeleton at the cell membrane may be a downstream effector of TRPV1 activation.