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. 2015 Jul 14;29(11):4532–4543. doi: 10.1096/fj.15-276493

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This is an Open Access article distributed under the terms of the Creative Commons Attribution 4.0 International (CC BY 4.0) (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Impact of palmitoylation on NCX1 trafficking and subcellular localization. A) Neither pharmacological nor genetic inhibition of NCX1 palmitoylation alters cell surface expression of NCX1 in stably transfected FT-293 cells (2-BP, 100 µM, applied overnight). B) Fractionation based on detergent solubility indicates YFP-NCX1-IC is membrane-anchored when palmitoylated in transiently transfected HEK cells. C) Subcellular distribution of YFP-NCX1-IC in transiently transfected HEK cells. Cys-less YFP-NCX1-IC is distributed similar to YFP alone. WT and C739^only YFP-NCX1-IC localize to an intracellular compartment but do not colocalize with the endoplasmic reticulum marker DsRed-ER. D) WT and C739^only YFP-NCX1-IC colocalize with the Golgi marker Grasp65-mCherry in transiently transfected HEK cells. E) NCX1 localizes to buoyant caveolin enriched microdomains in rat ventricular myocytes. F) Both palmitoylated and nonpalmitoylated NCX1 are present in buoyant caveolin enriched microdomains prepared from rat ventricular myocytes. 2-BP, 2-bromopalmitate; CS, cell surface protein; SM, starting cell lysate.