Bidirectional modulation of thermal and chemical sensitivity of TRPM8 channels by the initial region of the N-terminal domain

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Abstract

Background: The functional role of the TRPM8 N terminus remains poorly understood. Results: Truncation of the first 40 residues increases TRPM8 responses to cold and menthol, whereas deletions within the 40-60-residue region yield nonfunctional channels retained in the ER. Conclusion: Initial N terminus of TRPM8 is important for proper biogenesis and function. Significance: Variations within the N terminus can modulate thermal and chemical sensitivity of TRPM8. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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Pertusa, M., González, A., Hardy, P., Madrid, R., & Viana, F. (2014). Bidirectional modulation of thermal and chemical sensitivity of TRPM8 channels by the initial region of the N-terminal domain. Journal of Biological Chemistry, 289(32), 21828–21843. https://doi.org/10.1074/jbc.M114.565994

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