RGD Reference Report - Triadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubes. - Rat Genome Database

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Triadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubes.

Authors: Rezgui, SS  Vassilopoulos, S  Brocard, J  Platel, JC  Bouron, A  Arnoult, C  Oddoux, S  Garcia, L  De Waard, M  Marty, I 
Citation: Rezgui SS, etal., J Biol Chem. 2005 Nov 25;280(47):39302-8. Epub 2005 Sep 21.
RGD ID: 7327230
Pubmed: PMID:16176928   (View Abstract at PubMed)
PMCID: PMC2739420   (View Article at PubMed Central)
DOI: DOI:10.1074/jbc.M506566200   (Journal Full-text)

To identify the function of triadin in skeletal muscle, adenovirus-mediated overexpression of Trisk 95 or Trisk 51, the two major skeletal muscle isoforms, was induced in rat skeletal muscle primary cultures, and the physiological behavior of the modified cells was analyzed. Overexpression did not modify the expression level of their protein partners ryanodine receptor, dihydropyridine receptor, and the other triadin. Caffeine-induced calcium release was also unaffected by triadin overexpression. Nevertheless, in the absence of extracellular calcium, depolarization-induced calcium release was almost abolished in Trisk 95 overexpressing myotubes (T95 myotubes), and not modified in Trisk 51 overexpressing myotubes (T51 myotubes). This was not because of a modification of dihydropyridine receptors, as depolarization in presence of external calcium still induced a calcium release, and the activation curve of dihydropyridine receptor was unchanged, in both T95 and T51 myotubes. The calcium release complex was also maintained in T95 myotubes as Trisk 95, ryanodine receptor, dihydropyridine receptor, and Trisk 51 were still co-localized. The effect of Trisk 95 overexpression on depolarization-induced calcium release was reversed by a simultaneous infection with an antisense Trisk 95 adenovirus, indicating the specificity of this effect. Thus, the level of Trisk 95 and not Trisk 51 is important on regulating the calcium release complex, and an excess of this protein can lead to an inhibition of the physiological function of the complex.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
TrdnRatnegative regulation of release of sequestered calcium ion into cytosol  IMP  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Ryr1Ratprotein binding  IPITrdn (Rattus norvegicus) RGD 
TrdnRatprotein binding  IPIRyr1 (Rattus norvegicus) RGD 

Objects Annotated

Genes (Rattus norvegicus)
Ryr1  (ryanodine receptor 1)
Trdn  (triadin)


Additional Information