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. Author manuscript; available in PMC: 2018 Apr 17.
Published in final edited form as: J Am Coll Cardiol. 2018 Apr 3;71(13):1459–1470. doi: 10.1016/j.jacc.2018.01.060

FIGURE 7. Alcohol-Evoked JNK2 Regulates CaMKII Activity.

FIGURE 7

(A) Summarized data show increased ADP production (reflecting an increased ATP consumption in the CaMKII reaction with its substrate) in HA-pulldown CaMKII-WT proteins from alcohol-exposed cells, while JNK2I suppressed alcohol-evoked CaMKII activity. (B) Pooled ADP production assay data and representative immunoblotting images show that active pure JNK2 proteins increase the phosphorylation of CaMKII-WT, whereas autophosphorylation site mutation prevents this JNK2 action on HA-pulldown CaMKII-T286A proteins. (C) Summarized data show alcohol-enhanced CaMKII activity is not affected by the mutation of CaMKII oxidative sites Met280/281. (D) Summarized quantitative immunoblotting data and representative images show JNK2 inhibition prevented alcohol-enhanced phosphorylation of CaMKII (activated) in cultured HL-1 myocytes. CaMKII = calmodulin kinase; CaMKII-WT = wildtype CaMKII; CaMKII-T286A = CaMKII with Thr287Ala mutation; CaMKII-VV = CaMKII with Met280/281Val mutation; JNK2I = JNK2 inhibitor. Other abbreviations as in Figures 1 and 2.