de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors

Goswami,  Chandun
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50297

Hucho,  Tim
Signal 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;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8242-5
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.