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Physical interaction between calcineurin and Cav3.2 T‐type Ca 2 + channel modulates their functions
Author(s) -
Huang Ching-Hui,
Chen Yong-Cyuan,
Chen Chien-Chang
Publication year - 2013
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.2013.04.040
Subject(s) - calcineurin , nfat , calmodulin , phosphatase , chemistry , myocyte , muscle hypertrophy , biophysics , microbiology and biotechnology , biochemistry , endocrinology , biology , medicine , enzyme , transplantation
Ca v 3.2 T‐type Ca 2+ channel is required for the activation of calcineurin/NFAT signaling in cardiac hypertrophy. We aimed to investigate how Ca v 3.2 and calcineurin interact. We found that Ca 2+ and calmodulin modulate the Ca v 3.2/calcineurin interaction. Calcineurin binding to Ca v 3.2 decreases the enzyme's phosphatase activity and diminishes the channel's current density. Phenylephrine‐induced hypertrophy in neonatal cardiac myocytes is reduced by a cell‐permeable peptide with the calcineurin binding site sequence. These data suggest that Ca v 3.2 regulates calcineurin/NFAT pathway through both the Ca 2+ influx and calcineurin binding. Our findings unveiled a reciprocal regulation of Ca 2+ signaling which contributes to our understanding of cardiac hypertrophy.