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The Journal of Neuroscience, October 24, 2007, 27(43):11641-11650; doi:10.1523/JNEUROSCI.2457-07.2007

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Cellular/Molecular
A Role of the Transient Receptor Potential Domain of Vanilloid Receptor I in Channel Gating

Nuria García-Sanz,^1 * Pierluigi Valente,^1 * Ana Gomis,² Asia Fernández-Carvajal,¹ Gregorio Fernández-Ballester,¹ Felix Viana,² Carlos Belmonte,² and Antonio Ferrer-Montiel¹

¹Instituto de Biología Molecular y Celular and ²Instituto de Neurociencias de Alicante, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández, 03202 Elche, Alicante, Spain

Correspondence should be addressed to Antonio Ferrer-Montiel, Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Avenida de la Universidad s/n, 03202 Elche, Alicante, Spain. Email: aferrer{at}umh.es

Transient receptor potential vanilloid receptor subtype 1 (TRPV1) is an ionotropic receptor activated by temperature and chemical stimuli. The C-terminal region that is adjacent to the channel gate, recognized as the TRP domain, is a molecular determinant of receptor assembly. However, the role of this intracellular domain in channel function remains elusive. Here, we show that replacement of the TRP domain of TRPV1 with the cognate region of TRPV channels (TRPV2–TRPV6) did not affect receptor assembly and trafficking to the cell surface, although those receptors containing the TRP domain of the distantly related TRPV5 and TRPV6 did not display ion channel activity. Notably, functional chimeras exhibited an impaired sensitivity to the activating stimuli, consistent with a significant contribution of this protein domain to channel function. At variance with TRPV1, voltage-dependent gating of chimeric channels could not be detected in the absence of capsaicin and/or heat. Biophysical analysis of functional chimeras revealed that the TRP domain appears to act as a molecular determinant of the activation energy of channel gating. Together, these findings uncover a role of the TRP domain in intersubunit interactions near the channel gate that contribute to the coupling of stimulus sensing to channel opening.

Key words: channel gating; oligomerization; functional coupling; structure–function nociceptor; sensory transduction; capsaicin

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Received Jan. 8, 2007; revised Aug. 27, 2007; accepted Sept. 3, 2007.

Correspondence should be addressed to Antonio Ferrer-Montiel, Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, Avenida de la Universidad s/n, 03202 Elche, Alicante, Spain. Email: aferrer{at}umh.es

This article has been cited by other articles:

				M. Camprubi-Robles, R. Planells-Cases, and A. Ferrer-Montiel Differential contribution of SNARE-dependent exocytosis to inflammatory potentiation of TRPV1 in nociceptors FASEB J, November 1, 2009; 23(11): 3722 - 3733. [Abstract] [Full Text] [PDF]

				I. Hirschler-Laszkiewicz, Q. Tong, K. Conrad, W. Zhang, W. W. Flint, A. J. Barber, D. L. Barber, J. Y. Cheung, and B. A. Miller TRPC3 Activation by Erythropoietin Is Modulated by TRPC6 J. Biol. Chem., February 13, 2009; 284(7): 4567 - 4581. [Abstract] [Full Text] [PDF]

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