Correction: Structural basis of phosphatidylcholine recognition by the C2-Domain of cytosolic phospholipase A2α.

Errors have recently come to light regarding the descriptions of the model membranes used in fluorescence resonance energy transfer (FRET) experiments to compare the membrane partitioning of wild-type C2-domain versus Y96F, N65D, and Y96A C2-domain mutants. The errors involve Figures 3B, 3C, and 3D but do not alter the conclusions drawn from the FRET experiments. At the time of original publication, the model membranes used as energy acceptors in the FRET experiments were described as dansyl-PE/POPC/DHPC (5:45:50) bicelles. Based on more recent experiments performed for a 2020 Analytical Chemistry publication (Gao et al., 2020) and further elaborated in a recent (2021) Bio-protocol article (Gao et al., 2021), we now know that describing the energy acceptor model membranes as dansyl-PE/POPC/DHPC bicelles is incorrect. In the Analytical Chemistry paper, we showed that dilution of POPC-DHPC (50:50) 'bicelle' lipid mixes to the low micromolar range, as similarly employed and described in the Methods for the FRET experiments involving the C2-domain and mutants, results in nearly immediate transformation into small POPC unilamellar bilayer vesicles containing little or no DHPC. The transition reflects DHPC's high aqueous solubility. Thus, corrections have been introduced into the text (Methods) and the labels for the Figures 3B and 3C axes. We also have adjusted the Figure 3C X-axis label from "mM" to "mu M" as correctly conveyed in the original Methods section.