Key result
Recent studies using triadin knockout mice, human patients, and non-muscle cells suggest new scaffolding functions for triadin in regulating the ryanodine receptor complex.
This review proposes new hypotheses regarding the scaffolding functions of triadin within the ryanodine receptor complex in muscle cells.
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New triadin scaffolding hypotheses in RyR regulation should not yet alter practice; leaves open targeted mechanistic validation in cardiomyocytes.
The calcium release complex is the major player in excitation-contraction coupling, both in cardiac and skeletal muscle. The core of the complex is the ryanodine receptor, and triadin is a regulating protein. Nevertheless, the precise function of triadin is only partially understood. Besides its function in the anchoring of calsequestrin at the triad/dyad, our recent results allow us to propose hypotheses on new triadin scaffolding functions, based on the studies performed using different models, from triadin knockout mice to human patients, and expression in non-muscle cells, taking into account the presence of multiple triadin isoforms.
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Isabelle Marty (2014) reported a review. Triadin was evaluated. Recent studies using triadin knockout mice, human patients, and non-muscle cells suggest new scaffolding functions for triadin in regulating the ryanodine receptor complex.
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