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. 2019 Jun 25;10:2784. doi: 10.1038/s41467-019-10694-z

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Design and characterization of CaMKIIα-CaM association sensor. a Design of a FRET sensor for CaMKIIα-CaM association. Monomeric EGFP (mEGFP) and monomeric Cherry (mCherry) fluorescent protein are fused to the N-terminus of CaMKIIα and the N-terminus of CaM, respectively. b mCherry-CaM activates CaMKIIα to the degree similar to non-labeled CaM at different concentrations of CaM in a cell-free system. Upper panel: western blot of phosphorylated Synapsin1 peptide (pSyn1) fused to mCherry. Lower panel: quantification of pSyn1 signal from 4 experiments, normalized with the pSyn1 signal at 2 µM non-labeled CaM. c Fluorescence lifetime images of CaMKIIα-CaM association sensor expressed in HeLa cells. d Time courses of fluorescence lifetime of CaMKIIα-CaM association sensor and its mutants (T286A, T305D/T306D and T286D/T305A/T306A) in response to bath application of ionomycin (3 µM) and EGTA (10 mM). e Time courses of changes in CaMKIIα-CaM association calculated from d. All data are shown in mean ± sem