TRDN, also known as Triadin, is a transmembrane protein on the sarcoplasmic reticulum that encoded by human TRDN gene. Triadin also is a multiprotein family with four isoforms, denoted Trisk 95, Trisk 51, Trisk 49 and Trisk 32, which are arisen from the alternative splicing of TRDN gene on chromosome 6. Triadins belong to type II transmembrane proteins that are completely identical in their cytosolic and transmembrane domains, and they discriminate because of the length of their luminal domain and the sequence of their C-terminal end. It localizes in sarcoplasmic reticulum membrane and relates to the release of Ca2+ from the sarcoplasmic reticulum triggering muscular contraction through ca2+-induced cal2+ release.
|Basic Information of Triadin|
|Organism||Homo sapiens (Human)|
Triadin plays a significant role in the skeletal and heart muscle contraction, and in regulating the rate of heart beats. As a member of the calcium release complex, Triadin regulates lumenal Ca2+ release through the sarcoplasmic reticulum calcium release channels cardiac ryanodine receptor (RyR1) and ryanodine receptor (RYR2). Triadin is also able to sense luminal Ca2+ concentrations by mediating interactions between RYR2 and cardiac calsequestrin (CASQ2). The cardiac phenotype of Triadin knockout mice is quite similar to human patients affected by catecholaminergic polymorphic ventricular tachycardia. It has been confirmed that mutations in the TRDN gene resulted in severe human cardiac arrhythmia with sudden death, congenital myopathy, and skeletal muscle weakness.
Fig.1 Structure of the main triadin isoforms. (Marty, 2015)
This article presented human beings who have been confirmed to have biallelic pathogenic Triadin variants should be treated with anti-arrhythmic medications and given to defibrillator placement.
This article analyzed the skeletal muscle phenotype of the Triadin knockout syndrome by light and electron microscopy, immunohistochemical and clinical evaluation. And they found that absence of Triadin caused a congenital myopathy associated with profound pathologic alterations in components of the sarcoplasmic reticulum.
This article identified that cytoskeletonlinking membrane protein of 63 kDa (CLIMP-63) was the partner of Triadin that responsible for the association of triads and microtubules by using co-immunoprecipitation coupled to mass-spectrometry-based proteomics. They found that combination of triadin and CLIMP-63 could result in the formation of sarcoplasmic reticulum terminal cisternae and the guidance of microtubules close to the triads.
This article found out 3 amino acids which could influence Trisk 95 binding to RyR1 and ion channel activation. And results showed that Trisk 95 may not simultaneously bind to RyR1 and CSQ, which was different from the previous study that Triadin monomers form a quaternary complex with junction, CSQ, and RyR1.
This article described mutation in the TRDN gene caused arrhythmogenic phenotype with cardiac arrest and recurrent episodes of ventricular fibrillation despite β-blockade, which based on two siblings with cardiac arrest at young age.
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