Journal
JOURNAL OF NEUROCHEMISTRY
Volume 101, Issue 1, Pages 250-262Publisher
WILEY
DOI: 10.1111/j.1471-4159.2006.04338.x
Keywords
cytoskeleton; motif sequence; pain; receptor; TRPV; tubulin
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Previously, we reported that TRPV1, the vanilloid receptor, interacts with soluble alpha beta-tubulin dimers as well as microtubules via its C-terminal cytoplasmic domain. The interacting region of TRPV1, however, has not been defined. We found that the TRPV1 C-terminus preferably interacts with beta-tubulin and less with alpha-tubulin. Using a systematic deletion approach and bio-tinylated-peptides we identified two tubulin-binding sites present in TRPV1. These two sequence stretches are highly conserved in all known mammalian TRPV1 orthologues and partially conserved in some of the TRPV1 homologues. As these sequence stretches are not similar to any known tubulin-binding sequences, we conclude that TRPV1 interacts with tubulin and microtubule through two novel tubulin-binding motifs.
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