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Findings revealed that Ca2+ influx through L-type Ca(2+) channels (LTCCs) provides the immediate and efficient Ca2+ microdomain for the activation of SK channels. SK channel activation is predicted to provide a feedback mechanism to regulate the activities of LTCCs and RyR2 to influence the local and global Ca2+ signaling through the effects of SK channels on membrane potentials.
Study determined the three-dimensional structure of rabbit RyR2 in complex with the regulatory protein FKBP12.6 in the closed state at 11.8 A resolution using cryo-electron microscopy and built an atomic model of RyR2.
Two regions of the ryanodine receptor calcium channel are involved in Ca(2+)-dependent inactivation
[REVIEW] The efficacy of divalent calcium ion (Ca2+) release in the myocardium depends on the amount of Ca2+ loaded into the Ca2+ store and the way in which this Ca2* load influences the activity of the ryanodine receptor Ca2+ release channel (RyR2).
There were substantial transmural gradients in Cav1.2, KChIP2, ERG, KvLQT1, Kir2.1, NCX1, SERCA2a and RyR2 at the mRNA and, in some cases, protein level-in every case the mRNA or protein was more abundant in the epicardium than the endocardium.
comparison of key domains in InsP3 and ryanodine receptors
phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding.
results support a binding model where the CaM C-domain is anchored to RyR2 CaMBD2 and saturated with Ca(2+) during Ca(2+) oscillations, while the CaM N-domain functions as a dynamic Ca(2+) sensor that can bridge noncontiguous regions of RyR2 or clamp down onto CaMBD2.
Structural analysis revealed that the A165D mutation is located in a loop that is involved in inter-subunit interactions in the RyR2 tetrameric structure.
review of the molecular environment of individual amino acid residues that form binding sites for essential modulators of ion channel function and determine its role in Ca 2+ signalling.
We sought to identify genetic alterations in cardiac ion channels in patients with micro-ischemic disease. Genetic analysis with Sanger technology and posterior bioinformatic assessment identified two rare variations with potential pathogenic effects (RyR2_p.M4019T and SCN5A_p.H445D) in two individuals.
Genetic analysis of the index case identified only one rare novel variant p.Ile11Ser (c.32T>G) in the RyR2 gene. Subsequent familial analysis identified segregation of the genetic variant with the disease. To our knowledge, there has been no previous case report of catecholaminergic polymorphic ventricular tachycardia associated to this missense variant.
Our findings provided evidence that Indel polymorphism rs10692285 might contribute to sudden unexplained death (SUD) susceptibility through affecting the expression of RYR2, which suggest that abnormal ion channel activity is very likely to be the underlying mechanism of SUD.
Five of the 19 patients (26.3%) had either a pathogenic variant or a likely pathogenic variant in MYBPC3 (n=1), MYH7 (n=1), RYR2 (n=2), or TNNT2 (n=1). All five variants were missense variants that have been reported previously in patients with channelopathies or cardiomyopathies
RYR2 variants show possible pathogenic Fibrosis of the Cardiac Conduction system.
The most common form of CPVT is due to autosomal dominant variants in the cardiac ryanodine receptor gene (RYR2).
Common variants rs790899 and rs1891246 of RYR2 were significantly associated with HG and weight loss.
The left atrium / right atrium expression ratio was significantly increased in Atrial fibrillation for ryanodine receptor 2 - gene related to calcium uptake and release, and located on the sarcoplasmic reticulum membrane.
a direct interaction exists between RyR2 and CSQ2, is reported.
In a national cohort of RyR2 mutation-positive CPVT patients, SCD, ASCD and syncope were presenting events in the majority of probands and also occurred in 36% of relatives identified through family screening.
We identified a variant in the RYR2 gene (NM_001035) which involved a change of a glycine to an arginine in position155 of the gene product (c.463G > A, p.Gly155Arg, p.G155R). This RYR2 gene mutation is a novel rare genetic variant as it was not present in any of the international databases consulted.
Data suggest that post-translational modifications (phosphorylation, oxidation, and nitrosylation) of RyR2 (ryanodine receptor 2) occur downstream of production of amyloid beta-peptides through ADRB2 (beta2-adrenergic receptor) Ca2+ signaling cascade that activates PKA (protein kinase A).
The unique properties of the CaM-F142L mutation may provide novel clues on how to suppress excessive RyR2 Ca(2+) release by manipulating the CaM-RyR2 interaction.
Cardiac adrenergic response and progression towards HF proceed unaltered in mice harboring the RyR2-S2808A mutation. Preventing RyR2-S2808 phosphorylation does not preclude a normal sympathetic response nor mitigates the pathophysiological consequences of MI.
These results also suggest that altered cytosolic Ca(2+) activation of RyR2 represents a common defect of RyR2 mutations associated with catecholaminergic polymorphic ventricular tachycardia and atrial fibrillation, which could potentially be suppressed by carvedilol or (R)-carvedilol.
CaM and S100A1 can concurrently bind to and functionally modulate RyR1 and RyR2, but this does not involve direct competition at the RyR CaM binding site.
Long-Term Prognosis of Catecholaminergic Polymorphic Ventricular Tachycardia Patients With Ryanodine Receptor (RYR2) Mutations.
calsenilin controls the activity of neuronal RyRs.
These data demonstrate that the activity of RyR2, but not SERCA2a, is a major determinant of Ca2+ alternans in intact working mouse hearts.
distribution of RyR2 clusters in the periphery of live ventricular myocytes is irregular and dynamic
We found that this was caused by an abnormally tight interaction between CaMBD and mutated CaM-like domain (N4103K-CaMBD). Thus, CaMBD-CaMLD interaction may be a novel therapeutic target for treatment of lethal arrhythmia.
increased size of RyR2 protein clusters in vascular smooth muscle cells from mdx mice increases Ca(2+) spark and BK channel activity, resulting in cerebral microvascular dysfunction.
CaM dissociation may contribute to the pathogenesis of arrhythmias with the CPVT-linked R176Q mutation.
Reduced cardiac RyR2 expression protects against stress-induced ventricular tachyarrhythmia, but increases the susceptibility to cardiac alternans.
In this study, the large K(+) conductance of the RyR2 channel permits direct observation of blocking events as distinct subconductance states and for the first time demonstrates the differential effects of blocker molecules on channel gating.
In FHC-linked TnT-mutated hearts, RyR2 is susceptible to CaMKII-mediated phosphorylation, presumably because of a mutation-linked increase in diastolic [Ca(2+)]i, causing aberrant Ca(2+) release leading to lethal arrhythmia.
Genetically altered mice with congenitally leaky RyR2 exhibited premature and severe defects in synaptic plasticity, behavior and cognitive function.
A 3-fold increase in the junctophilin-2 to RyR2 ratio is compatible with direct inhibition of RyR2 opening by junctophilin-2 to intrinsically stabilize the Ca2+ signaling properties of the junction and thus the contractile function of the cell.
the coexistence of leaky RYR2 mutations with other genes that enhance epilepsy or cardiac arrhythmia establish RYR2 as a strong additional genetic candidate for sudden death risk.
the RyR2 G357S mutation increases the store overload induced Ca2+ release (SOICR) activity by reducing the thresholds for SOICR activation and termination and increasing the fractional Ca2+ release.
Arrhythmic effects of Epac-mediated ryanodine receptor activation in Langendorff-perfused murine hearts
K4750Q mutation causes three RyR2 defects: hypersensitization to activation by cytosolic Ca2+, loss of cytosolic Ca2+/Mg2+-mediated inactivation, and hypersensitization to luminal Ca2+ activation.
InsP3 dependent sarcoplasmic reticulum-Ca2+ flux constitute the main mechanism of functional crosstalk between InsP3R2 and RyR2 resulting in more Ca2+ sensitized RyRs to trigger subsequent Ca2+-induced Ca2+ release activation.
The heart contraction is controlled by the Ca2+-induced Ca2+ release between L-type Ca2+ channels and ryanodine receptors. RyRs became more sensitive to Ca2+ triggers without FKBP12.6, leading to ventricular arrthymias.
Allele-specific silencing of RYR2 prevents life-threatening arrhythmias in genetic carriers.
Redox modification of RyR2 synergistically with CaMKII phosphorylation modulates reperfusion arrhythmias.
This gene encodes a ryanodine receptor found in cardiac muscle sarcoplasmic reticulum. The encoded protein is one of the components of a calcium channel, composed of a tetramer of the ryanodine receptor proteins and a tetramer of FK506 binding protein 1B proteins, that supplies calcium to cardiac muscle. Mutations in this gene are associated with stress-induced polymorphic ventricular tachycardia and arrhythmogenic right ventricular dysplasia.
cardiac muscle ryanodine receptor
, ryanodine receptor 2 (cardiac)
, ryanodine receptor 2-like
, Ca2+ release channel
, cardiac muscle ryanodine receptor-calcium release channel
, cardiac muscle-type ryanodine receptor
, ryanodine receptor 2
, type 2 ryanodine receptor
, cardiac ryanodine receptor 2
, cardiac-type ryanodine receptor
, islet-type ryanodine receptor
, kidney-type ryanodine receptor
, ryanodine receptor type II
, calcium release channel
, ryanodine receptor type 2