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  Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1

Goswami, C., Hucho, T., & Hucho, F. (2007). Identification and characterisation of novel tubulin-binding motifs located within the C-terminus of TRPV1. Journal of Neurochemistry: Official Journal of the International Society for Neurochemistry, 101(1), 250-262. doi:10.1111/j.1471-4159.2006.04338.x.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8242-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8243-3
Genre: Journal Article
Alternative Title : J. Neurochem.

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 Creators:
Goswami, Chandun1, Author
Hucho, Tim2, Author              
Hucho, F., Author
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1Max Planck Society, ou_persistent13              
2Signal Transduction in Mental Retardation and Pain (Tim Hucho), Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479646              

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Free keywords: VDAC, voltage-dependent anion channel; TRP, transient receptor potential; MBP, maltose-binding protein; MT, microtubules; DMS, dimethyl suberimidate.
 Abstract: Previously, we reported that TRPV1, the vanilloid receptor, interacts with soluble αβ-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 β-tubulin and less with α-tubulin. Using a systematic deletion approach and biotinylated-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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Language(s): eng - English
 Dates: 2007-02-09
 Publication Status: Published in print
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Title: Journal of Neurochemistry : Official Journal of the International Society for Neurochemistry
  Alternative Title : J. Neurochem.
Source Genre: Journal
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Pages: - Volume / Issue: 101 (1) Sequence Number: - Start / End Page: 250 - 262 Identifier: ISSN: 1474-1644