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FLASH GENE

Symbol

TRDN

contributors: mct/npt - updated : 09-05-2017

HGNC name	triadin
HGNC id	12261

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

PROTEIN

PHYSICAL PROPERTIES

STRUCTURE

motifs/domains	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

HOMOLOGY

interspecies

homolog to C.elegans C14H10.2

intraspecies

homolog to ASPH

Homologene

FAMILY

CATEGORY

motor/contractile

SUBCELLULAR LOCALIZATION	plasma membrane,junction
	intracellular
	intracellular,cytoplasm,organelle,membrane
	intracellular,cytoplasm,organelle,endoplasmic reticulum
text	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

CELLULAR PROCESS

PHYSIOLOGICAL PROCESS

cardiovascular

PATHWAY

metabolism

signaling

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)

INTERACTION

DNA

RNA

small molecule

protein	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)
	CKAP4 is the partner of TRDN, and is responsible for the association of triads and microtubules
	association of TRDN and CKAP4 could be involved in the shaping of SR terminal cisternae and in the guidance of microtubules close to the triads

cell & other

REGULATION

Other

contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated (Milstein 2008)

ASSOCIATED DISORDERS

corresponding disease(s)

CPVT5

Other morbid association(s)

Type Gene Modification Chromosome rearrangement Protein expression Protein Function constitutional         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

Susceptibility

Variant & Polymorphism

Candidate gene

Marker

Therapy target

ANIMAL & CELL MODELS

triadin KO mouse presents objective muscle dysfunctions and is, therefore, undoubtedly suffering from myopathy as identical energy consumption produced a reduced strength (Oddoux 2009)