Goswami C, Hucho Tim B, Hucho F
Freie Universität Berlin, Institut für Chemie und Biochemie, Berlin, Germany.
J Neurochem. 2007 Apr;101(1):250-62. doi: 10.1111/j.1471-4159.2006.04338.x. Epub 2007 Feb 9.
Previously, we reported that TRPV1, the vanilloid receptor, interacts with soluble alphabeta-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 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.
此前，我们报道过香草酸受体TRPV1通过其C端胞质结构域与可溶性αβ-微管蛋白二聚体以及微管相互作用。然而，TRPV1的相互作用区域尚未明确。我们发现TRPV1的C端更倾向于与β-微管蛋白相互作用，与α-微管蛋白的相互作用较弱。通过系统缺失方法和生物素化肽段，我们在TRPV1中鉴定出两个微管蛋白结合位点。这两个序列片段在所有已知的哺乳动物TRPV1直系同源物中高度保守，在一些TRPV1同源物中部分保守。由于这些序列片段与任何已知的微管蛋白结合序列都不相似，我们得出结论，TRPV1通过两个新的微管蛋白结合基序与微管蛋白和微管相互作用。
