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The Journal of Neuroscience, May 3, 2006, 26(18):4835-4840; doi:10.1523/JNEUROSCI.5080-05.2006

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Brief Communications
A Hot-Sensing Cold Receptor: C-Terminal Domain Determines Thermosensation in Transient Receptor Potential Channels

Sebastian Brauchi,^1,2 Gerardo Orta,¹ Marcelo Salazar,¹ Eduardo Rosenmann,¹ and Ramon Latorre¹

¹Laboratory of Biophysics and Molecular Physiology, Centro de Estudios Cientificos and ²Universidad Austral de Chile, Valdivia, Chile 905-9100

Correspondence should be addressed to Dr. Ramon Latorre, Laboratory of Biophysics and Molecular Physiology, Centro de Estudios Científicos, Avenida Arturo Prat 514, Valdivia, Chile 905-9100. Email: rlatorre{at}cecs.cl

Temperature transduction in mammals is possible because of the presence of a set of temperature-dependent transient receptor potential (TRP) channels in dorsal root ganglia neurons and skin cells. Six thermo-TRP channels, all characterized by their unusually high temperature sensitivity (Q₁₀ > 10), have been cloned: TRPV1–4 are heat activated, whereas TRPM8 and TRPA1 are activated by cold. Because of the lack of structural information, the molecular basis for regulation by temperature remains unknown. In this study, we assessed the role of the C-terminal domain of thermo-TRPs and its involvement in thermal activation by using chimeras between the heat receptor TRPV1 and the cold receptor TRPM8, in which the entire C-terminal domain was switched. Here, we demonstrate that the C-terminal domain is modular and confers the channel phenotype regarding temperature sensitivity, channel gating kinetics, and PIP₂ (phosphatidylinositol-4,5-bisphophate) modulation. Thus, thermo-TRP channels contain an interchangeable specific region, different from the voltage sensor, which allows them to sense temperature stimuli.

Key words: TRPM8; TRPV1; chimeras; PIP₂; temperature activation; C-terminal domain

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Received Nov. 29, 2005; revised March 9, 2006; accepted March 21, 2006.

Correspondence should be addressed to Dr. Ramon Latorre, Laboratory of Biophysics and Molecular Physiology, Centro de Estudios Científicos, Avenida Arturo Prat 514, Valdivia, Chile 905-9100. Email: rlatorre{at}cecs.cl

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