Palmitoylation targets the Calcineurin phosphatase to the Phosphatidylinositol 4-kinase complex at the plasma membrane

This dataset is associated with the publication Ulengin-Talkish, I. et. al., 2021. This manuscript is currently under revision in Nature Communications. In this study, we elucidate a new signaling pathway regulated by the Ca2+-activated phosphatase, calcineurin (CN) by examining the understudied isoform CNAB1. Using multiple cell based biochemical assays including pulse-chase experiments with metabolic analog of palmitate and click chemistry, we show that CNAB1 is dynamically palmitoylated at two sites unique to its C-terminal tail. This dynamic palmitoylation, regulated by the ABHD17A depalmitoylase, confers unique localization to the plasma membrane (PM) and the golgi, substrate specificity and regulation to this isoform. We further uncover the PM-associated phosphatidylinositol 4-kinase complex to be a regulatory target of this isoform through which CN regulates PI4P production at the PM during signaling from the type-3 muscarinic receptor. This dataset specifically contains indirect immunofluorescence experiments done in COS-7 cells, which were used for the analysis shown in figures 1, 2 and supplementary figure 1. These multichannel images were acquired on a single z-plane on LionheartTM FX automated widefield microscope with a 20X Plan Fluorite WD 6.6 NP 0.45 objective.