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XB-ART-121
Neuron 2006 Jul 20;512:201-12. doi: 10.1016/j.neuron.2006.06.023.
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Coiled coils direct assembly of a cold-activated TRP channel.

Tsuruda PR, Julius D, Minor DL.


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Transient receptor potential (TRP) channels mediate numerous sensory transduction processes and are thought to function as tetramers. TRP channel physiology is well studied; however, comparatively little is understood regarding TRP channel assembly. Here, we identify an autonomously folded assembly domain from the cold- and menthol-gated channel TRPM8. We show that the TRPM8 cytoplasmic C-terminal domain contains a coiled coil that is necessary for channel assembly and sufficient for tetramer formation. Cell biological experiments indicate that coiled-coil formation is required for proper channel maturation and trafficking and that the coiled-coil domain alone can act as a dominant-negative inhibitor of functional channel expression. Our data define an authentic TRP modular assembly domain, establish a clear role for coiled coils in ion channel assembly, demonstrate that coiled-coil assembly domains are a general feature of TRPM channels, and delineate a new tool that should be of general use in dissecting TRPM channel function.

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Species referenced: Xenopus
Genes referenced: trpm8

References [+] :
Babila, Assembly of mammalian voltage-gated potassium channels: evidence for an important role of the first transmembrane segment. 1994, Pubmed, Xenbase