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The Journal of Neuroscience, July 11, 2007, 27(28):7578-7585; doi:10.1523/JNEUROSCI.1956-07.2007

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Cellular/Molecular
Contribution of the Putative Inner-Pore Region to the Gating of the Transient Receptor Potential Vanilloid Subtype 1 Channel (TRPV1)

Klara Susankova,¹ Rudiger Ettrich,² Ladislav Vyklicky,¹ Jan Teisinger,¹ and Viktorie Vlachova¹

¹Department of Cellular Neurophysiology, Institute of Physiology, Academy of Sciences of the Czech Republic, 142 20 Prague 4, Czech Republic, and ²Laboratory of High Performance Computing, Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic and Institute of Physical Biology, University of South Bohemia, 373 33 Nove Hrady, Czech Republic

Correspondence should be addressed to Dr. Viktorie Vlachova, Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic. Email: vlachova{at}biomed.cas.cz

The transient receptor potential vanilloid receptor-1 (TRPV1) is a sensory neuron-specific nonselective cation channel that is gated in response to various noxious stimuli: pungent vanilloids, low pH, noxious heat, and depolarizing voltages. By its analogy to K⁺ channels, the S6 inner helix domain of TRPV1 (Y666-G683) is a prime candidate to form the most constricted region of the permeation pathway and might therefore encompass an as-yet-unmapped gate of the channel. Using alanine-scanning mutagenesis, we identified 16 of 17 residues, that when mutated affected the functionality of the TRPV1 channel with respect to at least one stimulus modality. T670A was the only substitution producing the wild-type channel phenotype, whereas Y666A and N676A were nonfunctional but present at the plasma membrane. The periodicity of the functional effects of mutations within the TRPV1 inner pore region is consistent with an -helical structure in which T670 and A680 might play the roles of two bending "hinges."

Key words: capsaicin; vanilloid receptor; TRP channels; TRPV family; ion channel pores; structure–function relationship

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Received Feb. 1, 2007; revised May 30, 2007; accepted May 30, 2007.

Correspondence should be addressed to Dr. Viktorie Vlachova, Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic. Email: vlachova{at}biomed.cas.cz

This article has been cited by other articles:

				Y. Y. Wang, R. B. Chang, H. N. Waters, D. D. McKemy, and E. R. Liman The Nociceptor Ion Channel TRPA1 Is Potentiated and Inactivated by Permeating Calcium Ions J. Biol. Chem., November 21, 2008; 283(47): 32691 - 32703. [Abstract] [Full Text] [PDF]

				A. Jara-Oseguera, I. Llorente, T. Rosenbaum, and L. D. Islas Properties of the Inner Pore Region of TRPV1 Channels Revealed by Block with Quaternary Ammoniums J. Gen. Physiol., November 1, 2008; 132(5): 547 - 562. [Abstract] [Full Text] [PDF]

				J. A. Matta and G. P. Ahern Voltage is a partial activator of rat thermosensitive TRP channels J. Physiol., December 1, 2007; 585(2): 469 - 482. [Abstract] [Full Text] [PDF]

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