Hauptseite > Publikationsdatenbank > Anoctamin-4 is a bona fide Ca2+-dependent non-selective cation channel > print

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100 1 _ |a Reichhart, Nadine
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245 _ _ |a Anoctamin-4 is a bona fide Ca2+-dependent non-selective cation channel
260 _ _ |a [London]
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520 _ _ |a Changes in cell function occur by specific patterns of intracellular Ca2+, activating Ca2+-sensitive proteins. The anoctamin (TMEM16) protein family has Ca2+-dependent ion channel activity, which provides transmembrane ion transport, and/or Ca2+-dependent phosphatidyl-scramblase activity. Using amino acid sequence analysis combined with measurements of ion channel function, we clarified the so far unknown Ano4 function as Ca2+-dependent, non-selective monovalent cation channel; heterologous Ano4 expression in HEK293 cells elicits Ca2+ activated conductance with weak selectivity of K+ > Na+ > Li+. Endogenously expressed Ca2+-dependent cation channels in the retinal pigment epithelium were identified as Ano4 by KO mouse-derived primary RPE cells and siRNA against Ano4. Exchanging a negatively charged amino acid in the putative pore region (AA702–855) into a positive one (E775K) turns Ano4-elicited currents into Cl− currents evidencing its importance for ion selectivity. The molecular identification of Ano4 as a Ca2+-activated cation channel advances the understanding of its role in Ca2+ signaling.
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700 1 _ |a Schöberl, Simon
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700 1 _ |a Keckeis, Susanne
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700 1 _ |a Alfaar, Ahmad S.
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700 1 _ |a Roubeix, Christophe
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700 1 _ |a Cordes, Magdalena
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700 1 _ |a Crespo-Garcia, Sergio
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700 1 _ |a Haeckel, Akvile
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700 1 _ |a Kociok, Norbert
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700 1 _ |a Föckler, Renate
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700 1 _ |a Rauh, Robert
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700 1 _ |a Milenkovic, Vladimir M.
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700 1 _ |a Zühlke, Kerstin
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700 1 _ |a Klussmann, Enno
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700 1 _ |a Schellenberger, Eyk
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700 1 _ |a Strauß, Olaf
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773 _ _ |a 10.1038/s41598-018-37287-y
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