Ryanodine receptor 1 (RYR-1) also known as skeletal muscle calcium release channel or skeletal muscle-type ryanodine receptor is one of a class of ryanodine receptors and a protein found primarily in skeletal muscle. In humans, it is encoded by the RYR1gene.[5][6]
RYR1 functions as a calcium release channel in the sarcoplasmic reticulum, as well as a connection between the sarcoplasmic reticulum and the transverse tubule.[7] RYR1 is associated with the dihydropyridine receptor (L-type calcium channels) within the sarcolemma of the T-tubule, which opens in response to depolarization, and thus effectively means that the RYR1 channel opens in response to depolarization of the cell.
RYR1 plays a signaling role during embryonic skeletal myogenesis. A correlation exists between RYR1-mediated Ca2+ signaling and the expression of multiple molecules involved in key myogenic signaling pathways.[8] Of these, more than 10 differentially expressed genes belong to the Wnt family which are essential for differentiation. This coincides with the observation that without RYR1 present, muscle cells appear in smaller groups, are underdeveloped, and lack organization. Fiber type composition is also affected, with less type 1 muscle fibers when there are decreased amounts of RYR1.[9] These findings demonstrate RYR1 has a non-contractile role during muscle development.
RYR1 is mechanically linked to neuromuscular junctions for the calcium release-calcium induced biological process. While nerve-derived signals are required for acetylcholine receptor cluster distribution, there is evidence to suggest RYR1 activity is an important mediator in the formation and patterning of these receptors during embryological development.[10] The signals from the nerve and RYR1 activity appear to counterbalance each other. When RYR1 is eliminated, the acetylcholine receptor clusters appear in an abnormally narrow pattern, yet without signals from the nerve, the clusters are scattered and broad. Although their direct role is still unknown, RYR1 is required for proper distribution of acetylcholine receptor clusters.
Clinical significance
Mutations in the RYR1 gene are associated with malignant hyperthermia susceptibility, central core disease, minicore myopathy with external ophthalmoplegia and samaritan myopathy, a benign congenital myopathy.[11] Alternatively spliced transcripts encoding different isoforms have been demonstrated.[7]Dantrolene may be the only known drug that is effective during cases of malignant hyperthermia.[citation needed]
^ abcGRCh38: Ensembl release 89: ENSG00000196218 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000030592 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O'Brien PJ, MacLennan DH (July 1991). "Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia". Science. 253 (5018): 448–51. Bibcode:1991Sci...253..448F. doi:10.1126/science.1862346. PMID 1862346.
^Wu S, Ibarra MC, Malicdan MC, Murayama K, Ichihara Y, Kikuchi H, Nonaka I, Noguchi S, Hayashi YK, Nishino I (June 2006). "Central core disease is due to RYR1 mutations in more than 90% of patients". Brain. 129 (Pt 6): 1470–80. doi:10.1093/brain/awl077. PMID 16621918.
^Filipova D, Walter AM, Gaspar JA, Brunn A, Linde NF, Ardestani MA, Deckert M, Hescheler J, Pfitzer G, Sachinidis A, Papadopoulos S (April 2016). "Corrigendum: Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca(2+) release channel". Scientific Reports. 6: 24450. Bibcode:2016NatSR...624450F. doi:10.1038/srep24450. PMC4840354. PMID 27102063.
^Willemse H, Theodoratos A, Smith PN, Dulhunty AF (February 2016). "Unexpected dependence of RyR1 splice variant expression in human lower limb muscles on fiber-type composition". Pflügers Archiv. 468 (2): 269–78. doi:10.1007/s00424-015-1738-9. PMID 26438192. S2CID 5894066.
^Hanson MG, Niswander LA (December 2014). "An explant muscle model to examine the refinement of the synaptic landscape". Journal of Neuroscience Methods. 238: 95–104. doi:10.1016/j.jneumeth.2014.09.013. PMC4252626. PMID 25251554.
^Böhm J, Leshinsky-Silver E, Vassilopoulos S, Le Gras S, Lerman-Sagie T, Ginzberg M, Jost B, Lev D, Laporte J (October 2012). "Samaritan myopathy, an ultimately benign congenital myopathy, is caused by a RYR1 mutation". Acta Neuropathologica. 124 (4): 575–81. doi:10.1007/s00401-012-1007-3. PMID 22752422. S2CID 9014320.
^Fruen BR, Balog EM, Schafer J, Nitu FR, Thomas DD, Cornea RL (January 2005). "Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin". Biochemistry. 44 (1): 278–84. CiteSeerX10.1.1.578.9139. doi:10.1021/bi048246u. PMID 15628869.
^Cornea RL, Nitu F, Gruber S, Kohler K, Satzer M, Thomas DD, Fruen BR (April 2009). "FRET-based mapping of calmodulin bound to the RyR1 Ca2+ release channel". Proceedings of the National Academy of Sciences of the United States of America. 106 (15): 6128–33. Bibcode:2009PNAS..106.6128C. doi:10.1073/pnas.0813010106. PMC2662960. PMID 19332786.
^Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (June 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". The Journal of Biological Chemistry. 278 (25): 22600–8. doi:10.1074/jbc.M205866200. PMID 12704193.
^Bultynck G, De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys JB (March 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". The Biochemical Journal. 354 (Pt 2): 413–22. doi:10.1042/bj3540413. PMC1221670. PMID 11171121.
^Gaburjakova M, Gaburjakova J, Reiken S, Huang F, Marx SO, Rosemblit N, Marks AR (May 2001). "FKBP12 binding modulates ryanodine receptor channel gating". The Journal of Biological Chemistry. 276 (20): 16931–5. doi:10.1074/jbc.M100856200. PMID 11279144.
^Hwang SY, Wei J, Westhoff JH, Duncan RS, Ozawa F, Volpe P, Inokuchi K, Koulen P (August 2003). "Differential functional interaction of two Vesl/Homer protein isoforms with ryanodine receptor type 1: a novel mechanism for control of intracellular calcium signaling". Cell Calcium. 34 (2): 177–84. doi:10.1016/S0143-4160(03)00082-4. PMID 12810060.
^ abcFeng W, Tu J, Yang T, Vernon PS, Allen PD, Worley PF, Pessah IN (November 2002). "Homer regulates gain of ryanodine receptor type 1 channel complex". The Journal of Biological Chemistry. 277 (47): 44722–30. doi:10.1074/jbc.M207675200. PMID 12223488.
^Lee JM, Rho SH, Shin DW, Cho C, Park WJ, Eom SH, Ma J, Kim DH (February 2004). "Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin". The Journal of Biological Chemistry. 279 (8): 6994–7000. doi:10.1074/jbc.M312446200. PMID 14638677.
^Caswell AH, Motoike HK, Fan H, Brandt NR (January 1999). "Location of ryanodine receptor binding site on skeletal muscle triadin". Biochemistry. 38 (1): 90–7. doi:10.1021/bi981306+. PMID 9890886.
^Guo W, Campbell KP (April 1995). "Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum". The Journal of Biological Chemistry. 270 (16): 9027–30. doi:10.1074/jbc.270.16.9027. PMID 7721813.
^Groh S, Marty I, Ottolia M, Prestipino G, Chapel A, Villaz M, Ronjat M (April 1999). "Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor". The Journal of Biological Chemistry. 274 (18): 12278–83. doi:10.1074/jbc.274.18.12278. PMID 10212196.
Further reading
Treves S, Anderson AA, Ducreux S, Divet A, Bleunven C, Grasso C, Paesante S, Zorzato F (October 2005). "Ryanodine receptor 1 mutations, dysregulation of calcium homeostasis and neuromuscular disorders". Neuromuscular Disorders. 15 (9–10): 577–87. doi:10.1016/j.nmd.2005.06.008. PMID 16084090. S2CID 31372661.
ryanodine, receptor, also, known, skeletal, muscle, calcium, release, channel, skeletal, muscle, type, ryanodine, receptor, class, ryanodine, receptors, protein, found, primarily, skeletal, muscle, humans, encoded, ryr1, gene, ryr1identifiersaliasesryr1, mhs1,. Ryanodine receptor 1 RYR 1 also known as skeletal muscle calcium release channel or skeletal muscle type ryanodine receptor is one of a class of ryanodine receptors and a protein found primarily in skeletal muscle In humans it is encoded by the RYR1 gene 5 6 RYR1IdentifiersAliasesRYR1 CCO MHS MHS1 PPP1R137 RYDR RYR RYR 1 SKRR ryanodine receptor 1 KDSExternal IDsOMIM 180901 MGI 99659 HomoloGene 68069 GeneCards RYR1Gene location Human Chr Chromosome 19 human 1 Band19q13 2Start38 433 691 bp 1 End38 595 273 bp 1 Gene location Mouse Chr Chromosome 7 mouse 2 Band7 B1 7 16 94 cMStart29 003 344 bp 2 End29 125 179 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingastrocnemius muscletriceps brachii musclevastus lateralis muscletibialis anterior muscledeltoid musclethoracic diaphragmbody of tonguesural nerveamygdalacingulate gyrusTop expressed intriceps brachii musclevastus lateralis muscletemporal musclegastrocnemius muscleextensor digitorum longus muscleplantaris muscledigastric musclesternocleidomastoid muscleankleextraocular muscleMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionvoltage gated calcium channel activity calcium channel activity calmodulin binding protease binding ion channel activity protein binding enzyme binding calcium release channel activity ryanodine sensitive calcium release channel activity calcium induced calcium release activity calcium ion binding nucleotide binding ATP binding metal ion bindingCellular componentcytoplasm integral component of membrane membrane I band T tubule plasma membrane integral component of plasma membrane sarcoplasmic reticulum junctional sarcoplasmic reticulum membrane terminal cisterna smooth endoplasmic reticulum cell cortex junctional membrane complex extracellular exosome integral component of organelle membrane ryanodine receptor complex sarcoplasmic reticulum membrane Z disc cytoplasmic vesicle membrane protein containing complex calcium channel complex sarcolemmaBiological processossification involved in bone maturation regulation of cardiac conduction response to hypoxia muscle contraction release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of cytosolic calcium ion concentration outflow tract morphogenesis cellular calcium ion homeostasis ion transport multicellular organism development ion transmembrane transport skeletal muscle fiber development calcium ion transmembrane transport response to caffeine calcium ion transport skin development transmembrane transport cellular response to caffeine protein homotetramerization cellular response to calcium ion release of sequestered calcium ion into cytosol transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez626120190EnsemblENSG00000196218ENSMUSG00000030592UniProtP21817E9PZQ0RefSeq mRNA NM 000540NM 001042723NM 009109RefSeq protein NP 000531NP 001036188NP 033135Location UCSC Chr 19 38 43 38 6 MbChr 7 29 29 13 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Clinical significance 3 Interactions 4 See also 5 References 6 Further reading 7 External linksFunction EditRYR1 functions as a calcium release channel in the sarcoplasmic reticulum as well as a connection between the sarcoplasmic reticulum and the transverse tubule 7 RYR1 is associated with the dihydropyridine receptor L type calcium channels within the sarcolemma of the T tubule which opens in response to depolarization and thus effectively means that the RYR1 channel opens in response to depolarization of the cell RYR1 plays a signaling role during embryonic skeletal myogenesis A correlation exists between RYR1 mediated Ca2 signaling and the expression of multiple molecules involved in key myogenic signaling pathways 8 Of these more than 10 differentially expressed genes belong to the Wnt family which are essential for differentiation This coincides with the observation that without RYR1 present muscle cells appear in smaller groups are underdeveloped and lack organization Fiber type composition is also affected with less type 1 muscle fibers when there are decreased amounts of RYR1 9 These findings demonstrate RYR1 has a non contractile role during muscle development RYR1 is mechanically linked to neuromuscular junctions for the calcium release calcium induced biological process While nerve derived signals are required for acetylcholine receptor cluster distribution there is evidence to suggest RYR1 activity is an important mediator in the formation and patterning of these receptors during embryological development 10 The signals from the nerve and RYR1 activity appear to counterbalance each other When RYR1 is eliminated the acetylcholine receptor clusters appear in an abnormally narrow pattern yet without signals from the nerve the clusters are scattered and broad Although their direct role is still unknown RYR1 is required for proper distribution of acetylcholine receptor clusters Clinical significance EditMutations in the RYR1 gene are associated with malignant hyperthermia susceptibility central core disease minicore myopathy with external ophthalmoplegia and samaritan myopathy a benign congenital myopathy 11 Alternatively spliced transcripts encoding different isoforms have been demonstrated 7 Dantrolene may be the only known drug that is effective during cases of malignant hyperthermia citation needed Interactions EditRYR1 has been shown to interact with calmodulin 12 13 FKBP1A 14 15 16 HOMER1 17 18 HOMER2 18 HOMER3 18 and TRDN 19 20 21 22 See also EditRyanodine receptorReferences Edit a b c GRCh38 Ensembl release 89 ENSG00000196218 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000030592 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Fujii J Otsu K Zorzato F de Leon S Khanna VK Weiler JE O Brien PJ MacLennan DH July 1991 Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia Science 253 5018 448 51 Bibcode 1991Sci 253 448F doi 10 1126 science 1862346 PMID 1862346 Wu S Ibarra MC Malicdan MC Murayama K Ichihara Y Kikuchi H Nonaka I Noguchi S Hayashi YK Nishino I June 2006 Central core disease is due to RYR1 mutations in more than 90 of patients Brain 129 Pt 6 1470 80 doi 10 1093 brain awl077 PMID 16621918 a b Entrez Gene RYR1 ryanodine receptor 1 skeletal Filipova D Walter AM Gaspar JA Brunn A Linde NF Ardestani MA Deckert M Hescheler J Pfitzer G Sachinidis A Papadopoulos S April 2016 Corrigendum Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca 2 release channel Scientific Reports 6 24450 Bibcode 2016NatSR 624450F doi 10 1038 srep24450 PMC 4840354 PMID 27102063 Willemse H Theodoratos A Smith PN Dulhunty AF February 2016 Unexpected dependence of RyR1 splice variant expression in human lower limb muscles on fiber type composition Pflugers Archiv 468 2 269 78 doi 10 1007 s00424 015 1738 9 PMID 26438192 S2CID 5894066 Hanson MG Niswander LA December 2014 An explant muscle model to examine the refinement of the synaptic landscape Journal of Neuroscience Methods 238 95 104 doi 10 1016 j jneumeth 2014 09 013 PMC 4252626 PMID 25251554 Bohm J Leshinsky Silver E Vassilopoulos S Le Gras S Lerman Sagie T Ginzberg M Jost B Lev D Laporte J October 2012 Samaritan myopathy an ultimately benign congenital myopathy is caused by a RYR1 mutation Acta Neuropathologica 124 4 575 81 doi 10 1007 s00401 012 1007 3 PMID 22752422 S2CID 9014320 Fruen BR Balog EM Schafer J Nitu FR Thomas DD Cornea RL January 2005 Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2 sensitive acrylodan labeled calmodulin Biochemistry 44 1 278 84 CiteSeerX 10 1 1 578 9139 doi 10 1021 bi048246u PMID 15628869 Cornea RL Nitu F Gruber S Kohler K Satzer M Thomas DD Fruen BR April 2009 FRET based mapping of calmodulin bound to the RyR1 Ca2 release channel Proceedings of the National Academy of Sciences of the United States of America 106 15 6128 33 Bibcode 2009PNAS 106 6128C doi 10 1073 pnas 0813010106 PMC 2662960 PMID 19332786 Avila G Lee EH Perez CF Allen PD Dirksen RT June 2003 FKBP12 binding to RyR1 modulates excitation contraction coupling in mouse skeletal myotubes The Journal of Biological Chemistry 278 25 22600 8 doi 10 1074 jbc M205866200 PMID 12704193 Bultynck G De Smet P Rossi D Callewaert G Missiaen L Sorrentino V De Smedt H Parys JB March 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 The Biochemical Journal 354 Pt 2 413 22 doi 10 1042 bj3540413 PMC 1221670 PMID 11171121 Gaburjakova M Gaburjakova J Reiken S Huang F Marx SO Rosemblit N Marks AR May 2001 FKBP12 binding modulates ryanodine receptor channel gating The Journal of Biological Chemistry 276 20 16931 5 doi 10 1074 jbc M100856200 PMID 11279144 Hwang SY Wei J Westhoff JH Duncan RS Ozawa F Volpe P Inokuchi K Koulen P August 2003 Differential functional interaction of two Vesl Homer protein isoforms with ryanodine receptor type 1 a novel mechanism for control of intracellular calcium signaling Cell Calcium 34 2 177 84 doi 10 1016 S0143 4160 03 00082 4 PMID 12810060 a b c Feng W Tu J Yang T Vernon PS Allen PD Worley PF Pessah IN November 2002 Homer regulates gain of ryanodine receptor type 1 channel complex The Journal of Biological Chemistry 277 47 44722 30 doi 10 1074 jbc M207675200 PMID 12223488 Lee JM Rho SH Shin DW Cho C Park WJ Eom SH Ma J Kim DH February 2004 Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin The Journal of Biological Chemistry 279 8 6994 7000 doi 10 1074 jbc M312446200 PMID 14638677 Caswell AH Motoike HK Fan H Brandt NR January 1999 Location of ryanodine receptor binding site on skeletal muscle triadin Biochemistry 38 1 90 7 doi 10 1021 bi981306 PMID 9890886 Guo W Campbell KP April 1995 Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum The Journal of Biological Chemistry 270 16 9027 30 doi 10 1074 jbc 270 16 9027 PMID 7721813 Groh S Marty I Ottolia M Prestipino G Chapel A Villaz M Ronjat M April 1999 Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor The Journal of Biological Chemistry 274 18 12278 83 doi 10 1074 jbc 274 18 12278 PMID 10212196 Further reading EditTreves S Anderson AA Ducreux S Divet A Bleunven C Grasso C Paesante S Zorzato F October 2005 Ryanodine receptor 1 mutations dysregulation of calcium homeostasis and neuromuscular disorders Neuromuscular Disorders 15 9 10 577 87 doi 10 1016 j nmd 2005 06 008 PMID 16084090 S2CID 31372661 External links EditRYR1 protein human at the US National Library of Medicine Medical Subject Headings MeSH GeneReviews NIH UW entry on Multiminicore Disease GeneReviews NCBI NIH UW entry on Malignant Hyperthermia Susceptibility RYR1 Variation Database This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title Ryanodine receptor 1 amp oldid 1124526451, wikipedia, wiki, book, books, library,
