Biology:RYR3
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Generic protein structure example |
Ryanodine receptor 3 is a protein that in humans is encoded by the RYR3 gene.[1] The protein encoded by this gene is both a calcium channel and a receptor for the plant alkaloid ryanodine. RYR3 and RYR1 control the resting calcium ion concentration in skeletal muscle.[2]
See also
References
- ↑ "Localization of a novel ryanodine receptor gene (RYR3) to human chromosome 15q14-q15 by in situ hybridization". Genomics 18 (1): 163–5. Feb 1994. doi:10.1006/geno.1993.1446. PMID 8276408.
- ↑ "Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle". Am. J. Physiol., Cell Physiol. 288 (3): C640–9. March 2005. doi:10.1152/ajpcell.00407.2004. PMID 15548569.
Further reading
- Bertocchini F; Ovitt CE; Conti A et al. (1997). "Requirement for the ryanodine receptor type 3 for efficient contraction in neonatal skeletal muscles". EMBO J. 16 (23): 6956–63. doi:10.1093/emboj/16.23.6956. PMID 9384575.
- Bultynck G; De Smet P; Rossi D et al. (2001). "Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor". Biochem. J. 354 (Pt 2): 413–22. doi:10.1042/bj3540413. PMID 11171121.
- Schwarzmann N; Kunerth S; Weber K et al. (2002). "Knock-down of the type 3 ryanodine receptor impairs sustained Ca2+ signaling via the T cell receptor/CD3 complex". J. Biol. Chem. 277 (52): 50636–42. doi:10.1074/jbc.M209061200. PMID 12354756.
- Nakashima Y; Nishimura S; Maeda A et al. (1997). "Molecular cloning and characterization of a human brain ryanodine receptor". FEBS Lett. 417 (1): 157–62. doi:10.1016/S0014-5793(97)01275-1. PMID 9395096.
- Xiao B; Masumiya H; Jiang D et al. (2002). "Isoform-dependent formation of heteromeric Ca2+ release channels (ryanodine receptors)". J. Biol. Chem. 277 (44): 41778–85. doi:10.1074/jbc.M208210200. PMID 12213830.
- Davis MR; Haan E; Jungbluth H et al. (2003). "Principal mutation hotspot for central core disease and related myopathies in the C-terminal transmembrane region of the RYR1 gene". Neuromuscul. Disord. 13 (2): 151–7. doi:10.1016/S0960-8966(02)00218-3. PMID 12565913.
- Kitahara K; Kawa S; Katsuyama Y et al. (2008). "Microsatellite scan identifies new candidate genes for susceptibility to alcoholic chronic pancreatitis in Japanese patients". Dis. Markers 25 (3): 175–80. doi:10.1155/2008/426764. PMID 19096130.
- Tochigi M; Kato C; Ohashi J et al. (2008). "No association between the ryanodine receptor 3 gene and autism in a Japanese population". Psychiatry Clin. Neurosci. 62 (3): 341–4. doi:10.1111/j.1440-1819.2008.01802.x. PMID 18588595.
- Masumiya H; Yamamoto H; Hemberger M et al. (2003). "The mouse sino-atrial node expresses both the type 2 and type 3 Ca(2+) release channels/ryanodine receptors". FEBS Lett. 553 (1–2): 141–4. doi:10.1016/S0014-5793(03)00999-2. PMID 14550562.
- "Smooth muscle tissues express a major dominant negative splice variant of the type 3 Ca2+ release channel (ryanodine receptor)". J. Biol. Chem. 278 (7): 4763–9. 2003. doi:10.1074/jbc.M210410200. PMID 12471029.
- Mohaupt MG; Karas RH; Babiychuk EB et al. (2009). "Association between statin-associated myopathy and skeletal muscle damage". Canadian Medical Association Journal 181 (1–2): E11–8. doi:10.1503/cmaj.081785. PMID 19581603.
- Balschun D; Wolfer DP; Bertocchini F et al. (1999). "Deletion of the ryanodine receptor type 3 (RyR3) impairs forms of synaptic plasticity and spatial learning". EMBO J. 18 (19): 5264–73. doi:10.1093/emboj/18.19.5264. PMID 10508160.
- "Partial cloning and differential expression of ryanodine receptor/calcium-release channel genes in human tissues including the hippocampus and cerebellum". Neuroscience 85 (1): 205–16. 1998. doi:10.1016/S0306-4522(97)00612-X. PMID 9607712.
- Ota T; Suzuki Y; Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Van Acker K; Bultynck G; Rossi D et al. (2004). "The 12 kDa FK506-binding protein, FKBP12, modulates the Ca(2+)-flux properties of the type-3 ryanodine receptor". J. Cell Sci. 117 (Pt 7): 1129–37. doi:10.1242/jcs.00948. PMID 14970260.
- Bultynck G; Rossi D; Callewaert G et al. (2001). "The conserved sites for the FK506-binding proteins in ryanodine receptors and inositol 1,4,5-trisphosphate receptors are structurally and functionally different". J. Biol. Chem. 276 (50): 47715–24. doi:10.1074/jbc.M106573200. PMID 11598113.
- "cDNA cloning and sequencing of the human ryanodine receptor type 3 (RYR3) reveals a novel alternative splice site in the RYR3 gene". FEBS Lett. 423 (3): 367–70. 1998. doi:10.1016/S0014-5793(98)00124-0. PMID 9515741.
- Lynn S; Morgan JM; Lamb HK et al. (1995). "Isolation and partial cloning of ryanodine-sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle". FEBS Lett. 372 (1): 6–12. doi:10.1016/0014-5793(95)00924-X. PMID 7556644.
External links
- RYR3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)