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   <subfield code="a">Lobe-related concentration- and Ca2+-dependent interactions of calmodulin with C- and N-terminal tails of the CaV1.2 channel</subfield>
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   <subfield code="c">[Guilin He, Feng Guo, Tong Zhu, Dongxue Shao, Rui Feng, Dandan Yin, Xuefei Sun, Huiyuan Hu, Ahhyeon Hwang, Etsuko Minobe, Masaki Kameyama, Liying Hao]</subfield>
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   <subfield code="a">This study examined the bindings of calmodulin (CaM) and its mutants with the C- and N-terminal tails of the voltage-gated Ca2+ channel CaV1.2 at different CaM and Ca2+ concentrations ([Ca2+]) by using the pull-down assay method to obtain basic information on the binding mode, including its concentration- and Ca2+-dependencies. Our data show that more than one CaM molecule could bind to the CaV1.2 C-terminal tail at high [Ca2+]. Additionally, the C-lobe of CaM is highly critical in sensing the change of [Ca2+] in its binding to the C-terminal tail of CaV1.2, and the binding between CaM and the N-terminal tail of CaV1.2 requires high [Ca2+]. Our data provide new details on the interactions between CaM and the CaV1.2 channel.</subfield>
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