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The Journal of Neuroscience, June 9, 2004, 24(23):5307-5314; doi:10.1523/JNEUROSCI.0202-04.2004

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Cellular/Molecular
Identification of a Tetramerization Domain in the C Terminus of the Vanilloid Receptor

Nuria García-Sanz, Asia Fernández-Carvajal, Cruz Morenilla-Palao, Rosa Planells-Cases, Emmanuel Fajardo-Sánchez, Gregorio Fernández-Ballester, and Antonio Ferrer-Montiel

Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, 03202 Alicante, Spain

TRPV1 (transient receptor potential vanilloid receptor subtype 1) is a member of the TRP channel family gated by vanilloids, protons, and heat. Structurally, TRPV1 appears to be a tetramer formed by the assembly of four identical subunits around a central aqueous pore. The molecular determinants that govern its subunit oligomerization remain elusive. Here, we report the identification of a segment comprising ⁶⁸⁴Glu-⁷²¹Arg (referred to as the TRP-like domain) in the C terminus of TRPV1 as an association domain (AD) of the protein. Purified recombinant C terminus of TRPV1 (TRPV1-C) formed discrete and stable multimers in vitro. Yeast two-hybrid and pull-down assays showed that self-association of the TRPV1-C is blocked when segment ⁶⁸⁴Glu-⁷²¹Arg is deleted. Biochemical and immunological analysis indicate that removal of the AD from full-length TRPV1 monomers blocks the formation of stable heteromeric assemblies with wild-type TRPV1 subunits. Deletion of the AD in a poreless TRPV1 subunit suppressed its robust dominant-negative phenotype. Together, these findings are consistent with the tenet that the TRP-like domain in TRPV1 is a molecular determinant of the tetramerization of receptor subunits into functional channels. Our observations suggest that the homologous TRP domain in the TRP protein family may function as a general, evolutionary conserved AD involved in subunit multimerization.

Key words: ion channel; oligomerization; TRP domain; nociceptors; sensory transduction; synaptic transmission

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Received Jan 19, 2004; revised March 27, 2004; accepted April 16, 2004.

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