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| Item Type: | Article |
|---|---|
| Title: | Anoctamin-4 is a bona fide Ca(2+)-dependent non-selective cation channel |
| Creators Name: | Reichhart, N., Schöberl, S., Keckeis, S., Alfaar, A.S., Roubeix, C., Cordes, M., Crespo-Garcia, S., Haeckel, A., Kociok, N., Föckler, R., Fels, G., Mataruga, A., Rauh, R., Milenkovic, V.M., Zühlke, K., Klussmann, E., Schellenberger, E. and Strauß, O. |
| Abstract: | Changes in cell function occur by specific patterns of intracellular Ca(2+), activating Ca(2+)-sensitive proteins. The anoctamin (TMEM16) protein family has Ca(2+)-dependent ion channel activity, which provides transmembrane ion transport, and/or Ca(2+)-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 Ca(2+)-dependent, non-selective monovalent cation channel; heterologous Ano4 expression in HEK293 cells elicits Ca(2+) activated conductance with weak selectivity of K(+) > Na(+) > Li(+). Endogenously expressed Ca(2+)-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 Ca(2+)-activated cation channel advances the understanding of its role in Ca(2+) signaling. |
| Keywords: | Anoctamins, Calcium, Calcium Channels, Cations, HEK293 Cells, Knockout Mice, Animals, Mice |
| Source: | Scientific Reports |
| ISSN: | 2045-2322 |
| Publisher: | Nature Publishing Group |
| Volume: | 9 |
| Number: | 1 |
| Page Range: | 2257 |
| Date: | 19 February 2019 |
| Official Publication: | https://doi.org/10.1038/s41598-018-37287-y |
| PubMed: | View item in PubMed |
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