General Physiology and Biophysics Vol.41, No.2, p. 133–140, 2022
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Title: Junctophilin-2 allosterically interacts with ryanodine receptor type 2 to regulate calcium release units in mouse cardiomyocytes |
Author: Tianxia Luo, Ningning Yan, Mengru Xu, Fengjuan Dong, Qian Liang, Ying Xing, Hongkun Fan |
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Abstract: The interaction between junctophilin-2 (JPH2) and ryanodine receptor type 2 (RyR2) regulated Ca2+ signaling in mouse cardiomyocytes. However, their exact interaction remains unclear. This study elucidates the interaction between JPH2 with RyR2 using co-immunoprecipitation of cardiac sarcoplasmic reticulum vesicles. Additionally, a glutathione S-transferase (GST) pull-down analysis was performed to investigate the physical interaction between RyR2 and JPH2 fragments. JPH2 interacted with RyR2 and the C terminus of the JPH2 protein can pull-down RyR2 receptors. Confocal immunofluorescence imaging indicated that the majority of JPH2 and RyR2 proteins were colocalized near Z-lines in isolated mouse cardiomyocytes. Knockdown of JPH2 reduced the amplitude of Ca2+ transients and disrupted its interaction with RyR2. Therefore, the C-terminus domain of JPH2 is required for interactions with RyR2 in mouse cardiomyocytes, which provides a molecular mechanism for seeking Ca2+-related disease prevention strategies.
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Keywords: unctophilin-2 — Ryanodine receptor type 2 — Cardiomyocytes — Ca2+ release |
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Published online: 11-Apr-2022
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Year: 2022, Volume: 41, Issue: 2 |
Page From: 133, Page To: 140 |
doi:10.4149/gpb_2022007
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