RYR1

Ryanodine receptor 1 (skeletal)

PDB rendering based on 2bcx.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2bcx

Identifiers

Symbols

RYR1 ; CCO; MHS; MHS1; PPP1R137; RYDR; RYR; RYR-1; SKRR

External IDs

OMIM: 180901 MGI: 99659 HomoloGene: 68069 IUPHAR: 747 ChEMBL: 1846 GeneCards: RYR1 Gene

Gene ontology
Molecular function	• protease binding • ryanodine-sensitive calcium-release channel activity • voltage-gated calcium channel activity • calcium channel activity • protein binding • calmodulin binding • calcium-release channel activity
Cellular component	• cytoplasm • smooth endoplasmic reticulum • cytosol • plasma membrane • integral component of plasma membrane • cell cortex • junctional sarcoplasmic reticulum membrane • terminal cisterna • sarcoplasmic reticulum • junctional membrane complex • T-tubule • I band • sarcoplasmic reticulum membrane • extracellular exosome
Biological process	• response to hypoxia • outflow tract morphogenesis • calcium ion transport • muscle contraction • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • response to caffeine • ion transmembrane transport • skin development • ossification involved in bone maturation • skeletal muscle fiber development • release of sequestered calcium ion into cytosol • cytosolic calcium ion homeostasis • transmembrane transport • calcium ion transmembrane transport • cellular response to caffeine
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
38.43 – 38.59 Mb

Chr 7:
29 – 29.13 Mb

PubMed search

Ryanodine receptor 1 (RYR-1) also known as skeletal muscle calcium release channel or skeletal muscle-type ryanodine receptor is a protein found primarily in skeletal muscle. In humans, it is encoded by the RYR1 gene.^[1]^[2]

Function

RYR1 functions as a calcium release channel in the sarcoplasmic reticulum, as well as a connection between the sarcoplasmic reticulum and the transverse tubule.^[3]

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.^[4] Alternatively spliced transcripts encoding different isoforms have been demonstrated.^[3] Dantrolene may be the only known drug that is effective during cases of malignant hyperthermia.

Interactions

RYR1 has been shown to interact with:

References

↑ Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O'Brien PJ, MacLennan DH (Jul 1991). "Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia". Science 253 (5018): 448–51. 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 (Jun 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.
1 2 "Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)".
↑ Böhm J, Leshinsky-Silver E, Vassilopoulos S, Le Gras S, Lerman-Sagie T, Ginzberg M, Jost B, Lev D, Laporte J (Oct 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.
↑ Fruen BR, Balog EM, Schafer J, Nitu FR, Thomas DD, Cornea RL (Jan 2005). "Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin". Biochemistry 44 (1): 278–84. doi:10.1021/bi048246u. PMID 15628869.
↑ Cornea RL, Nitu F, Gruber S, Kohler K, Satzer M, Thomas DD, Fruen BR (Apr 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. doi:10.1073/pnas.0813010106. PMC 2662960. PMID 19332786.
↑ Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (Jun 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 (Mar 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 (Aug 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.
1 2 3 Feng W, Tu J, Yang T, Vernon PS, Allen PD, Worley PF, Pessah IN (Nov 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 (Feb 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 (Jan 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 (Apr 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 (Apr 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.

External links

RYR1 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

PDB gallery

2bcx: Crystal structure of calmodulin in complex with a ryanodine receptor peptide

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Ligand-gated	Inositol trisphosphate receptor 1 2 3 Ryanodine receptor 1 2 3

Voltage-gated	L-type/Ca_vα 1.1 1.2 1.3 1.4 N-type/Ca_vα2.2 P-type/Ca_vα 2.1 Q-type/Ca_vα2.1 R-type/Ca_vα2.3 T-type/Ca_vα 3.1 3.2 3.3 α₂δ-subunits 1 2 β-subunits β1 β2 β3 β4 γ-subunits γ1 γ2 γ3 γ4 Cation channels of sperm 1 2 3 4 Two-pore channel 1 2

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel α β γ δ

Proton-gated	Amiloride-sensitive cation channel 1 2 3 4

Voltage-gated	Na_vα 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 7A Na_vβ 1 2 3 4

K⁺: Potassium channel

Calcium-activated	BK channel α1 β1 β2 β3 β4 SK channel SK1 SK2 SK3 IK channel IK1 K_Ca 1.1 2.1 2.2 2.3 3.1 4.1 4.2 5.1

Inward-rectifier	K_ATP K_ir 1.1 2.1 2.2 2.3 2.4 2.6 GIRK/K_ir 3.1 3.2 3.3 3.4 K_ir 4.1 4.2 5.1 6.1 6.2 7.1

Tandem pore domain	K2P 1 2 3 4 5 6 7 9 10 12 13 15 16 17 18

Voltage-gated	K_vα1-6 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 2.1 2.2 3.1 3.2 3.3 3.4 4.1 4.2 4.3 5.1 6.1 6.2 6.3 6.4 K_vα7-12 7.1 7.2 7.3 7.4 7.5 8.1 8.2 9.1 9.2 9.3 10.1 10.2 11.1/hERG 11.2 11.3 12.1 12.2 12.3 K_vβ 1 2 3 KCNIP 1 2 3 4 minK/ISK minK/ISK-like MiRP 1 2 3 Shaker gene

Miscellaneous

Cl⁻: Chloride channel	Calcium-activated chloride channels Anoctamin ANO1 Bestrophin 1 2 Chloride Channel Accessory 1 2 3 4 CFTR CLCN 1 2 3 4 5 6 7 KA KB CLIC 1 2 3 4 5 6 L1 CLNS 1A 1B

H⁺: Proton channel	HVCN1

M⁺: CNG cation channel	α 1 2 3 4 β 1 2 3 HCN FC 1 2 3 4

M⁺: TRP cation channel	TRPA (1) TRPC 1 2 3 4 4AP 5 6 7 TRPM 1 2 3 4 5 6 7 8 TRPML 1 2 3 TRPN TRPP 1 2 TRPV 1 2 3 4 5 6

H₂O (+ solutes): Porin	Aquaporin 0 1 2 3 4 5 6 7 8 9 Voltage-dependent anion channel 1 2 3 General bacterial porin family

Cytoplasm: Gap junction	Connexin: A GJA1 GJA3 GJA4 GJA5 GJA8 GJA9 GJA10 B GJB1 GJB2 GJB3 GJB4 GJB5 GJB6 GJB7 C GJC1 GJC2 GJC3 D GJD2 GJD3 GJD4) Innexin

By gating mechanism

Ion channel class	Ligand-gated Light-gated Voltage-gated Stretch-activated

see also disorders

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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