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. 2018 Aug 7;9:1081. doi: 10.3389/fphys.2018.01081

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Copyright © 2018 Tanaka, Fujio and Nakayama.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Caveolae-specific CaMKII activation was detectable using phosphor-peptide tags. (A) Schematic diagram of a fusion protein comprised of the cytosolic domain of phospholamban (cPLN) and caveolin-3 (Cav3). (B) Phosphorylation at threonine 17 of the cytosolic domain of phospholamban in the fusion protein and endogenous phospholamban. The fusion protein comprised of cPLN and caveolin-3 (cPLN-Cav3) was expressed by adenoviral gene transfer in neonatal rat cardiomyocytes (NRCMs). After 15 min of β-adrenergic stimulation with isoproterenol (ISO) at the indicated concentration, cells were harvested and their protein extracts were prepared. The phosphorylation of phospholamban at threonine 17 (Thr17), the CaMKII-specific phosphorylation site, was assessed using a phospho-specific antibody for Thr17 of PLN, and its level was enhanced in a dose-dependent manner in both cPLN-Cav3 (upper arrow) and endogenous PLN (lower arrow). The membrane was re-probed using an anti-PLN antibody. (C) Schema of the proposed method for caveolae-specific CaMKII activation using a fusion protein and phospho-specific antibody. CaMKII activation induced by β-adrenergic stimulation provokes phosphorylation of cPLN-Cav3, which is localized in caveolae.