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Nature 455, 1210-1215 (30 October 2008) | doi:10.1038/nature07313; Received 16 May 2008; Accepted 5 August 2008; Published online 24 August 2008
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TMEM16A confers receptor-activated calcium-dependent chloride conductance
Young Duk Yang1, Hawon Cho1, Jae Yeon Koo1, Min Ho Tak1, Yeongyo Cho1, Won-Sik Shim1, Seung Pyo Park1, Jesun Lee1, Byeongjun Lee1, Byung-Moon Kim1, Ramin Raouf2, Young Ki Shin1 & Uhtaek Oh1
- Sensory Research Center, CRI, College of Pharmacy, Seoul National University, Seoul 151-742, Korea
- Molecular Nociception Group, Neuroscience, Physiology and Pharmacology, University College London, London WC1E 6BT, UK
Correspondence to: Uhtaek Oh1 Correspondence and requests for materials should be addressed to U.O. (Email: utoh@snu.ac.kr).
Abstract
Calcium (Ca2+)-activated chloride channels are fundamental mediators in numerous physiological processes including transepithelial secretion, cardiac and neuronal excitation, sensory transduction, smooth muscle contraction and fertilization. Despite their physiological importance, their molecular identity has remained largely unknown. Here we show that transmembrane protein 16A (TMEM16A, which we also call anoctamin 1 (ANO1)) is a bona fide Ca2+-activated chloride channel that is activated by intracellular Ca2+ and Ca2+-mobilizing stimuli. With eight putative transmembrane domains and no apparent similarity to previously characterized channels, ANO1 defines a new family of ionic channels. The biophysical properties as well as the pharmacological profile of ANO1 are in full agreement with native Ca2+-activated chloride currents. ANO1 is expressed in various secretory epithelia, the retina and sensory neurons. Furthermore, knockdown of mouse Ano1 markedly reduced native Ca2+-activated chloride currents as well as saliva production in mice. We conclude that ANO1 is a candidate Ca2+-activated chloride channel that mediates receptor-activated chloride currents in diverse physiological processes.
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