Goswami C, Dreger M, Jahnel R, Bogen O, Gillen C, Hucho F
Freie Universität Berlin, Institute für Chemie-Biochemie, Berlin, Germany.
J Neurochem. 2004 Dec;91(5):1092-103. doi: 10.1111/j.1471-4159.2004.02795.x.
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 Ca2+ -signalling events. In a proteomic screen for proteins associated with the C-terminal sequence of TRPV1, we identified beta-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 Ca2+ -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 Ca2+ -sensitivity of this interaction suggests that the microtubule cytoskeleton at the cell membrane may be a downstream effector of TRPV1 activation.
香草酸受体TRPV1在检测一系列化学和热有害刺激（如与组织炎症及由此产生的疼痛相关的刺激）中发挥着既定的功能作用。TRPV1激活会导致膜去极化，但也可能引发细胞内Ca2+信号事件。在一项针对与TRPV1 C端序列相关蛋白质的蛋白质组学筛选中，我们鉴定出β-微管蛋白是一种特异性与TRPV1相互作用的蛋白质。我们证明，TRPV1 C端尾部能够结合微管蛋白二聚体，也能结合聚合的微管。这种相互作用对Ca2+敏感，并影响微管特性，如微管对低温和诺考达唑的敏感性。因此，我们的数据为TRPV1与细胞骨架的相互作用提供了有力证据。这种相互作用对Ca2+的敏感性表明，细胞膜处的微管细胞骨架可能是TRPV1激活的下游效应器。
