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. 2011 Sep;1808(9):2214–2223. doi: 10.1016/j.bbamem.2011.05.017

Fig. 1.

Fig. 1

TMEM16A(0) as a membrane protein associated with anion transport activity. A. Topology of TMEM16A with localization of alternative segments a, b, and c (top) and immunofluorescence analysis of 16A(0) and 16A(abc) subcellular localization (bottom). Images were taken from stable transfected or from null FRT cells. B. Representative traces (top) and summary of data (bottom) from experiments carried out with the YFP assay on HEK-293 cells transiently transfected with TMEM16A isoforms or empty plasmids. Red and blue traces show the cell fluorescence decrease following I− addition (arrow) with and without 1 μM ionomycin, respectively. The bar graph reports the maximal quenching rate (QR) by I−. ***, p < 0.001 vs. null cells (n = 6–13). C. Representative traces and statistics from transepithelial Cl− current experiments. The graph reports the peak current elicited by 1 μM ionomycin. ***, p < 0.001 vs. null cells (n = 13–35).