Abstract
Calumenin is a multiple EF-hand Ca2+-binding protein localized in the sarcoplasmic reticulum (SR). In our recent study, we showed that calumenin-knockdown (KD) of HL-1 cells led to enhanced Ca2+ release and Ca2+ uptake in the SR (Sahoo et. al. J. Biol. Chem., 2009). To elucidate the underlying mechanisms responsible for the enhanced Ca2+ release from the SR in calumenin-KD samples, the possible interaction between calumenin and RyR2 was examined by various methods. GST pull-down assay showed a direct interaction between calumenin and RyR2. We have further found that the middle region of calumenin (aa 132-222) interacts with RyR2. GST pull-down assay also shows that RyR2 intra luminal loop-I region (aa 4519-4576) is the binding site for calumenin. Immunofluorescence study shows that RyR2 and calumenin are co-localized in the junctional region of SR in rat ventricular cardiomyocytes. The detailed amino acid residues involved in the interaction between calumenin and RyR2 are currently under investigation. (This work was supported by the Korean Ministry of Science and Technology grant, Systems Biology Research Grant, M1050301001-6N0301-0110, and the 2009 GIST Systems Biology Infrastructure Establishment Grant).
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