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Symbol TRDN contributors: mct/npt - updated : 09-05-2016
HGNC name triadin
HGNC id 12261
Corresponding disease
CPVT5 catecholaminergic polymorphic ventricular tachycardia 5, with or without muscle weakness
Location 6q22.31      Physical location : 123.537.482 - 123.957.942
Synonym name triadin skeletal 51
Synonym symbol(s) SMTRD, TDN, TRIADIN, TRISK, TRISK51, MGC88285, DKFZp779I2253, dJ166D18.1 (triadin), CPVT5
TYPE functioning gene
STRUCTURE 420.75 kb     41 Exon(s)
10 Kb 5' upstream gene genomic sequence study
MAPPING cloned Y linked   status provisional
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
- - - 95 - cardiac 2012 22505613
  • able to block the depolarization-induced calcium release
  • located within the triad and associated with RyR
  • when ectopically expressed, Trisk 95 can modulate reticulum membrane morphology
  • TRISK95 200-231 region is responsible for RYR1 activation (PMID: 22937102)
  • 21 - 4763 51 463 major triadin isoform expressed in human skeletal muscle 2012 22505613
  • also called TRISK51
  • located within the triad and associated with RyR
  • 41 - 4782 - 729 - 2012 22505613
    9 - 1864 32 297 - 2012 22505613
  • also called TRISK32
  • 1020p100 of all triadins
  • mainly in the longitudinal sarcoplasmic reticulum associated with the inositol trisphosphate receptor
  • its overexpression had no effect on store-operated Ca(2+) entry, despite a decrease in the expression of STIM1
  • not only co-localizes with, but directly contributes to, the regulation of Ca(2+) release via IP(3)R (PMID: 21811790)
  • 9 - 3002 - 286 - 2012 22505613
    6 - 1413 - 167 - 2012 22505613
    Type widely
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularheart   highly
    Respiratoryrespiratory tractlarynx  highly
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Muscularstriatumcardiac highly
    Muscularstriatumskeletal highly
    cell lineage
    cell lines
    at STAGE
  • a transmembrane segment including repeated KEKE (GLU-LYS-GLU-LYS) motifs important for macromolecular protein-protein interactions within their SR luminal tails (Fan 2008)
  • a short cytoplasmic tail
  • three regions, named TR1 (targeting region 1), TR2 and TR3, that contribute to the localization of triadin at the j-SR (junctional domain of the sarcoplasmic reticulum), and TR3 contains binding sites for CASQ1 and triadin clustering can be enhanced by binding to CASQ1
    interspecies homolog to C.elegans C14H10.2
    intraspecies homolog to ASPH
    CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     plasma membrane,junction
    intracellular,cytoplasm,organelle,endoplasmic reticulum
  • junction of sarcoplasmic reticulum type II membrane protein
  • with CASQ2, are located in specialized areas of the sarcoplasmic reticulum (SR) where the SR forms junctions with the sarcolemma (junctional SR) (Knollmann 2009)
  • basic FUNCTION
  • putatively involved in excitation/contraction coupling
  • may be be involved in the set up and maintenance of a precise sarcoplasmic reticulum structure
  • may be involved in anchoring calsequestrin to the junctional sarcoplasmic reticulum and allowing its functional coupling with the ryanodine receptor
  • indirect role for triadin in regulating myoplasmic Ca(2+) homeostasis and organizing the molecular complex of the triad but not in regulating skeletal-type excitation-contraction coupling (Shen 2007)
  • with CASQ2 are important for the structural organization of the SR (Knollmann 2009)
  • triadin and junctin are integral sarcoplasmic reticulum membrane proteins that form a macromolecular complex with the skeletal muscle ryanodine receptor (RYR1) (Wang 2009)
  • has a role in facilitating KCl depolarization-induced Ca2+ release in contrast to junctin which has a role in maintaining sarcoplasmic reticulum Ca2+ store size in myotubes (Wang 2009)
  • ASPH and TRDN each activate skeletal ryanodine receptors but ASPH alone mediates functional interactions with CASQ1
  • importance of triadin for the normal function of the cardiac calcium release complex
  • TRDN and ASPH are structurally related transmembrane proteins thought to be key mediators of structural and functional interactions between calsequestrin (CASQ1) and ryanodine receptor (RyRs) at the junctional sarcoplasmic reticulum
    PHYSIOLOGICAL PROCESS cardiovascular
    a component
  • homooligomer of variable subunit number, disulfide-linked
  • CASQ2, TRDN and ASPH form a protein complex that is associated with cardiac ryanodine receptor 2 (RYR2) SR Ca(2+) release channels (Knollmann 2009)
  • could be involved in maintaining triads during contraction, and in anchoring mitochondria close to triads (Oddoux 2009)
  • is an essential link within the calcium release complex (Oddoux 2009)
    small molecule
  • binding and anchoring calsequestrin to the ryanodine receptor
  • interaction between RYR1 and triadin could play an active role in the overall Ca2+ release process of excitation-contraction coupling in muscle cells
  • role for CASQ1 in promoting the stable association of TRDN to the multiprotein complex associated with RYR
  • CASQ2, HRC and RYR2 share the same KEKE motif region on the distal part of TRDN (aa 202-231)
  • cell & other
    Other contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated (Milstein 2008)
    corresponding disease(s) CPVT5
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    displayed extensive T-wave inversions in precordial leads V1 through V4, with either persistent or transient QT prolongation and severe disease expression of exercise-induced cardiac arrest in early childhood
    Variant & Polymorphism
    Candidate gene
    Therapy target
    triadin KO mouse presents objective muscle dysfunctions and is, therefore, undoubtedly suffering from myopathy as identical energy consumption produced a reduced strength (Oddoux 2009)