Ryanodine receptor 2

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Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Ryanodine receptor 2 (RYR2) is one of a class of ryanodine receptors and a protein found primarily in cardiac muscle. In humans, it is encoded by the RYR2 gene.[1][2][3] In the process of cardiac calcium-induced calcium release, RYR2 is the major mediator for sarcoplasmic release of stored calcium ions.

Structure

The channel is composed of RYR2 homotetramers and FK506-binding proteins found in a 1:4 stoichiometric ratio. Calcium channel function is affected by the specific type of FK506 isomer interacting with the RYR2 protein, due to binding differences and other factors.[4]

Function

The RYR2 protein functions as the major component of a calcium channel located in the sarcoplasmic reticulum that supplies ions to the cardiac muscle during systole. To enable cardiac muscle contraction, calcium influx through voltage-gated L-type calcium channels in the plasma membrane allows calcium ions to bind to RYR2 located on the sarcoplasmic reticulum. This binding causes the release of calcium through RYR2 from the sarcoplasmic reticulum into the cytosol, where it binds to the C domain of troponin, which shifts tropomyosin and allows the myosin ATPase to bind to actin, enabling cardiac muscle contraction.[5] RYR2 channels are associated with many cellular functions, including mitochondrial metabolism, gene expression and cell survival, in addition to their role in cardiomyocyte contraction.[6]

Clinical significance

Deleterious mutations of the ryanodine receptor family, and especially the RYR2 receptor, lead to a constellation of pathologies leading to both acute and chronic heart failure collectively known as "Ryanopathies."[7]

Mutations in the RYR2 gene are associated with catecholaminergic polymorphic ventricular tachycardia and arrhythmogenic right ventricular dysplasia.[8]

Recently, sudden cardiac death in several young individuals in the Amish community (four of which were from the same family) was traced to homozygous duplication of a mutant RyR2 gene.[9] Normal (wild type) RyR2 functions primarily in the myocardium (heart muscle).

Mice with genetically reduced RYR2 exhibit a lower basal heart rate and fatal arrhythmias.[10]

Interactions

Ryanodine receptor 2 has been shown to interact with:

See also

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Otsu K, Willard HF, Khanna VK, Zorzato F, Green NM, MacLennan DH (August 1990). "Molecular cloning of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum". The Journal of Biological Chemistry. 265 (23): 13472–13483. doi:10.1016/S0021-9258(18)77371-7. PMID 2380170.
  2. ^ Page Module:Citation/CS1/styles.css has no content.Otsu K, Fujii J, Periasamy M, Difilippantonio M, Uppender M, Ward DC, et al. (August 1993). "Chromosome mapping of five human cardiac and skeletal muscle sarcoplasmic reticulum protein genes". Genomics. 17 (2): 507–509. doi:10.1006/geno.1993.1357. PMID 8406504.
  3. ^ Page Module:Citation/CS1/styles.css has no content.Tiso N, Stephan DA, Nava A, Bagattin A, Devaney JM, Stanchi F, et al. (February 2001). "Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2)". Human Molecular Genetics. 10 (3): 189–194. doi:10.1093/hmg/10.3.189. hdl:11577/2459215. PMID 11159936.
  4. ^ Page Module:Citation/CS1/styles.css has no content.Guo T, Cornea RL, Huke S, Camors E, Yang Y, Picht E, et al. (June 2010). "Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks". Circulation Research. 106 (11): 1743–1752. doi:10.1161/CIRCRESAHA.110.219816. PMC 2895429. PMID 20431056.
  5. ^ Page Module:Citation/CS1/styles.css has no content."Q92736 - RYR2_HUMAN".
  6. ^ Page Module:Citation/CS1/styles.css has no content.Bround MJ, Wambolt R, Luciani DS, Kulpa JE, Rodrigues B, Brownsey RW, et al. (June 2013). "Cardiomyocyte ATP production, metabolic flexibility, and survival require calcium flux through cardiac ryanodine receptors in vivo". The Journal of Biological Chemistry. 288 (26): 18975–18986. doi:10.1074/jbc.M112.427062. PMC 3696672. PMID 23678000.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Belevych AE, Radwański PB, Carnes CA, Györke S (May 2013). "'Ryanopathy': causes and manifestations of RyR2 dysfunction in heart failure". Cardiovascular Research. 98 (2): 240–247. doi:10.1093/cvr/cvt024. PMC 3633158. PMID 23408344.
  8. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: RYR2 ryanodine receptor 2 (cardiac)".
  9. ^ Page Module:Citation/CS1/styles.css has no content.Tester DJ, Bombei HM, Fitzgerald KK, Giudicessi JR, Pitel BA, Thorland EC, et al. (March 2020). "Identification of a Novel Homozygous Multi-Exon Duplication in RYR2 Among Children With Exertion-Related Unexplained Sudden Deaths in the Amish Community". JAMA Cardiology. 5 (3): 13–18. doi:10.1001/jamacardio.2019.5400. PMC 6990654. PMID 31913406.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Bround MJ, Asghari P, Wambolt RB, Bohunek L, Smits C, Philit M, et al. (December 2012). "Cardiac ryanodine receptors control heart rate and rhythmicity in adult mice". Cardiovascular Research. 96 (3): 372–380. doi:10.1093/cvr/cvs260. PMC 3500041. PMID 22869620.
  11. ^ a b c d Page Module:Citation/CS1/styles.css has no content.Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, et al. (May 2000). "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts". Cell. 101 (4): 365–376. doi:10.1016/S0092-8674(00)80847-8. PMID 10830164. S2CID 6496567.
  12. ^ Page Module:Citation/CS1/styles.css has no content.Marx SO, Reiken S, Hisamatsu Y, Gaburjakova M, Gaburjakova J, Yang YM, et al. (May 2001). "Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers". The Journal of Cell Biology. 153 (4): 699–708. doi:10.1083/jcb.153.4.699. PMC 2192391. PMID 11352932.
  13. ^ a b c Page Module:Citation/CS1/styles.css has no content.Huke S, Bers DM (November 2008). "Ryanodine receptor phosphorylation at Serine 2030, 2808 and 2814 in rat cardiomyocytes". Biochemical and Biophysical Research Communications. 376 (1): 80–85. doi:10.1016/j.bbrc.2008.08.084. PMC 2581610. PMID 18755143.
  14. ^ Page Module:Citation/CS1/styles.css has no content.Witcher DR, Kovacs RJ, Schulman H, Cefali DC, Jones LR (June 1991). "Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity". The Journal of Biological Chemistry. 266 (17): 11144–11152. doi:10.1016/S0021-9258(18)99140-4. PMID 1645727.
  15. ^ Page Module:Citation/CS1/styles.css has no content.Wehrens XH, Lehnart SE, Reiken SR, Marks AR (April 2004). "Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor". Circulation Research. 94 (6): e61–e70. doi:10.1161/01.RES.0000125626.33738.E2. PMID 15016728.
  16. ^ Page Module:Citation/CS1/styles.css has no content.Meyers MB, Pickel VM, Sheu SS, Sharma VK, Scotto KW, Fishman GI (November 1995). "Association of sorcin with the cardiac ryanodine receptor". The Journal of Biological Chemistry. 270 (44): 26411–26418. doi:10.1074/jbc.270.44.26411. PMID 7592856.

Further reading

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