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The individual N‐ and C‐lobes of calmodulin tether to the Cav1.2 channel and rescue the channel activity from run‐down in ventricular myocytes of guinea‐pig heart
Author(s) -
Shao Dongxue,
Zhao Meimi,
Xu Jianjun,
Feng Rui,
Guo Feng,
Hu Huiyuan,
Sun Xuefei,
Gao Qinghua,
He Guilin,
Sun Wei,
Wang Hongmei,
Yu Lifeng,
Liu Suyuan,
Zhu Yaonan,
Minobe Etsuko,
Zhu Tong,
Kameyama Masaki,
Hao Liying
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.029
Subject(s) - calmodulin , cav1.2 , basal (medicine) , calcium channel , guinea pig , myocyte , biophysics , chemistry , anatomy , medicine , calcium , biology , microbiology and biotechnology , endocrinology , insulin
The present study examined the binding of the individual N‐ and C‐lobes of calmodulin (CaM) to Cav1.2 at different Ca 2+ concentration ([Ca 2+ ]) from ≈ free to 2 mM, and found that they may bind to Cav1.2 Ca 2+ ‐dependently. In particular, using the patch‐clamp technique, we confirmed that the N‐ or C‐lobes can rescue the basal activity of Cav1.2 from run‐down, demonstrating the functional relevance of the individual lobes. The data imply that at resting [Ca 2+ ], CaM may tether to the channel with its single lobe, leading to multiple CaM molecule binding to increase the grade of Ca 2+ ‐dependent regulation of Cav1.2.