RYR2

RYR2
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	4JKQ
Identifikatori
Aliasi	RYR2
Vanjski ID-jevi	OMIM: 180902 MGI: 99685 HomoloGene: 37423 GeneCards: RYR2
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	237,833,988 bp
Lokacija gena (miš)
Hrom.	Hromosom 13 (miš)
Kraj	12,106,945 bp
Ontologija gena
Molekularna funkcija	• transmembrane transporter binding; • calcium channel activity; • calcium-induced calcium release activity; • protein kinase A catalytic subunit binding; • organic cyclic compound binding; • protein self-association; • ion channel activity; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje identičnih proteina; • vezivanje enzima; • suramin binding; • protein kinase A regulatory subunit binding; • protein kinase binding; • calcium-release channel activity; • ryanodine-sensitive calcium-release channel activity; • calcium ion binding; • calmodulin binding;
Ćelijska komponenta	• integral component of membrane; • Kalcijski kanal; • membrana; • Sarkomera; • junctional sarcoplasmic reticulum membrane; • Sarkoplazmatski retikulum; • Z discdkac; • sarcoplasmic reticulum membrane; • smooth endoplasmic reticulum; • ćelijska membrana; • GO:0009327 makromolekulani kompleks; • cytoplasmic vesicle membrane; • Sarkolema;
Biološki proces	• response to muscle stretch; • release of sequestered calcium ion into cytosol; • calcium ion transport into cytosol; • regulation of cardiac conduction; • regulation of cardiac muscle contraction by calcium ion signaling; • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; • response to hypoxia; • cardiac muscle contraction; • regulation of cytosolic calcium ion concentration; • positive regulation of the force of heart contraction; • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; • cardiac muscle hypertrophy; • ventricular cardiac muscle cell action potential; • cell communication by electrical coupling involved in cardiac conduction; • cellular calcium ion homeostasis; • establishment of protein localization to endoplasmic reticulum; • ion transport; • BMP signaling pathway; • left ventricular cardiac muscle tissue morphogenesis; • regulation of heart rate; • positive regulation of heart rate; • detection of calcium ion; • response to redox state; • cellular response to epinephrine stimulus; • multicellular organism development; • ion transmembrane transport; • positive regulation of sequestering of calcium ion; • embryonic heart tube morphogenesis; • calcium ion transmembrane transport; • cellular response to caffeine; • sarcoplasmic reticulum calcium ion transport; • canonical Wnt signaling pathway; • regulation of SA node cell action potential; • response to caffeine; • regulation of cardiac muscle contraction; • regulation of ventricular cardiac muscle cell action potential; • regulation of AV node cell action potential; • calcium-mediated signaling using intracellular calcium source; • response to muscle activity; • calcium ion transport; • calcium-mediated signaling; • type B pancreatic cell apoptotic process; • regulation of atrial cardiac muscle cell action potential; • positive regulation of ATPase-coupled calcium transmembrane transporter activity; • Purkinje myocyte to ventricular cardiac muscle cell signaling; • transmembrane transport;
	Izvori:Amigo / QuickGO
Ortolozi
	6262
	20191
	ENSG00000198626
	ENSMUSG00000021313
	Q92736
	E9Q401
	NM_001035
	NM_023868
	NP_001026
	NP_076357
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Rijanodinski receptor 2 (RYR2) je protein koji je prvenstveno nađen u miokardnim mišićima. Kod ljudi kodiran je genom RYR2.^[5]^[6]^[7] U procesu srčanog oslobađanja kalcija inducirano kalcijem, RYR2 je glavni posrednik za sarkoplazmatsko oslobađanje uskladištenih iona kalcija.

Struktura

Kanal se sastoji od RYR2 homotetramera i FK506-vezujućih proteina koji su u stehiometrijskom omjeru 1: 4. Na funkciju kalcijevih kanala utiče specifični tip izomera FK506 koji djeluje u interakciji s proteinom RYR2, zbog razlika u vezanju i drugih faktora.^[8]

Aminokiselinska sekvenca

10	20	30	40	50
MADGGEGEDE	IQFLRTDDEV	VLQCTATIHK	EQQKLCLAAE	GFGNRLCFLE
STSNSKNVPP	DLSICTFVLE	QSLSVRALQE	MLANTVEKSE	GQVDVEKWKF
MMKTAQGGGH	RTLLYGHAIL	LRHSYSGMYL	CCLSTSRSST	DKLAFDVGLQ
EDTTGEACWW	TIHPASKQRS	EGEKVRVGDD	LILVSVSSER	YLHLSYGNGS
LHVDAAFQQT	LWSVAPISSG	SEAAQGYLIG	GDVLRLLHGH	MDECLTVPSG
EHGEEQRRTV	HYEGGAVSVH	ARSLWRLETL	RVAWSGSHIR	WGQPFRLRHV
TTGKYLSLME	DKNLLLMDKE	KADVKSTAFT	FRSSKEKLDV	GVRKEVDGMG
TSEIKYGDSV	CYIQHVDTGL	WLTYQSVDVK	SVRMGSIQRK	AIMHHEGHMD
DGISLSRSQH	EESRTARVIR	STVFLFNRFI	RGLDALSKKA	KASTVDLPIE
SVSLSLQDLI	GYFHPPDEHL	EHEDKQNRLR	ALKNRQNLFQ	EEGMINLVLE
CIDRLHVYSS	AAHFADVAGR	EAGESWKSIL	NSLYELLAAL	IRGNRKNCAQ
FSGSLDWLIS	RLERLEASSG	ILEVLHCVLV	ESPEALNIIK	EGHIKSIISL
LDKHGRNHKV	LDVLCSLCVC	HGVAVRSNQH	LICDNLLPGR	DLLLQTRLVN
HVSSMRPNIF	LGVSEGSAQY	KKWYYELMVD	HTEPFVTAEA	THLRVGWAST
EGYSPYPGGG	EEWGGNGVGD	DLFSYGFDGL	HLWSGCIART	VSSPNQHLLR
TDDVISCCLD	LSAPSISFRI	NGQPVQGMFE	NFNIDGLFFP	VVSFSAGIKV
RFLLGGRHGE	FKFLPPPGYA	PCYEAVLPKE	KLKVEHSREY	KQERTYTRDL
LGPTVSLTQA	AFTPIPVDTS	QIVLPPHLER	IREKLAENIH	ELWVMNKIEL
GWQYGPVRDD	NKRQHPCLVE	FSKLPEQERN	YNLQMSLETL	KTLLALGCHV
GISDEHAEDK	VKKMKLPKNY	QLTSGYKPAP	MDLSFIKLTP	SQEAMVDKLA
ENAHNVWARD	RIRQGWTYGI	QQDVKNRRNP	RLVPYTLLDD	RTKKSNKDSL
REAVRTLLGY	GYNLEAPDQD	HAARAEVCSG	TGERFRIFRA	EKTYAVKAGR
WYFEFETVTA	GDMRVGWSRP	GCQPDQELGS	DERAFAFDGF	KAQRWHQGNE
HYGRSWQAGD	VVGCMVDMNE	HTMMFTLNGE	ILLDDSGSEL	AFKDFDVGDG
FIPVCSLGVA	QVGRMNFGKD	VSTLKYFTIC	GLQEGYEPFA	VNTNRDITMW
LSKRLPQFLQ	VPSNHEHIEV	TRIDGTIDSS	PCLKVTQKSF	GSQNSNTDIM
FYRLSMPIEC	AEVFSKTVAG	GLPGAGLFGP	KNDLEDYDAD	SDFEVLMKTA
HGHLVPDRVD	KDKEATKPEF	NNHKDYAQEK	PSRLKQRFLL	RRTKPDYSTS
HSARLTEDVL	ADDRDDYDFL	MQTSTYYYSV	RIFPGQEPAN	VWVGWITSDF
HQYDTGFDLD	RVRTVTVTLG	DEKGKVHESI	KRSNCYMVCA	GESMSPGQGR
NNNGLEIGCV	VDAASGLLTF	IANGKELSTY	YQVEPSTKLF	PAVFAQATSP
NVFQFELGRI	KNVMPLSAGL	FKSEHKNPVP	QCPPRLHVQF	LSHVLWSRMP
NQFLKVDVSR	ISERQGWLVQ	CLDPLQFMSL	HIPEENRSVD	ILELTEQEEL
LKFHYHTLRL	YSAVCALGNH	RVAHALCSHV	DEPQLLYAIE	NKYMPGLLRA
GYYDLLIDIH	LSSYATARLM	MNNEYIVPMT	EETKSITLFP	DENKKHGLPG
IGLSTSLRPR	MQFSSPSFVS	ISNECYQYSP	EFPLDILKSK	TIQMLTEAVK
EGSLHARDPV	GGTTEFLFVP	LIKLFYTLLI	MGIFHNEDLK	HILQLIEPSV
FKEAATPEEE	SDTLEKELSV	DDAKLQGAGE	EEAKGGKRPK	EGLLQMKLPE
PVKLQMCLLL	QYLCDCQVRH	RIEAIVAFSD	DFVAKLQDNQ	RFRYNEVMQA
LNMSAALTAR	KTKEFRSPPQ	EQINMLLNFK	DDKSECPCPE	EIRDQLLDFH
EDLMTHCGIE	LDEDGSLDGN	SDLTIRGRLL	SLVEKVTYLK	KKQAEKPVES
DSKKSSTLQQ	LISETMVRWA	QESVIEDPEL	VRAMFVLLHR	QYDGIGGLVR
ALPKTYTING	VSVEDTINLL	ASLGQIRSLL	SVRMGKEEEK	LMIRGLGDIM
NNKVFYQHPN	LMRALGMHET	VMEVMVNVLG	GGESKEITFP	KMVANCCRFL
CYFCRISRQN	QKAMFDHLSY	LLENSSVGLA	SPAMRGSTPL	DVAAASVMDN
NELALALREP	DLEKVVRYLA	GCGLQSCQML	VSKGYPDIGW	NPVEGERYLD
FLRFAVFCNG	ESVEENANVV	VRLLIRRPEC	FGPALRGEGG	NGLLAAMEEA
IKIAEDPSRD	GPSPNSGSSK	TLDTEEEEDD	TIHMGNAIMT	FYSALIDLLG
RCAPEMHLIH	AGKGEAIRIR	SILRSLIPLG	DLVGVISIAF	QMPTIAKDGN
VVEPDMSAGF	CPDHKAAMVL	FLDRVYGIEV	QDFLLHLLEV	GFLPDLRAAA
SLDTAALSAT	DMALALNRYL	CTAVLPLLTR	CAPLFAGTEH	HASLIDSLLH
TVYRLSKGCS	LTKAQRDSIE	VCLLSICGQL	RPSMMQHLLR	RLVFDVPLLN
EHAKMPLKLL	TNHYERCWKY	YCLPGGWGNF	GAASEEELHL	SRKLFWGIFD
ALSQKKYEQE	LFKLALPCLS	AVAGALPPDY	MESNYVSMME	KQSSMDSEGN
FNPQPVDTSN	ITIPEKLEYF	INKYAEHSHD	KWSMDKLANG	WIYGEIYSDS
SKVQPLMKPY	KLLSEKEKEI	YRWPIKESLK	TMLAWGWRIE	RTREGDSMAL
YNRTRRISQT	SQVSVDAAHG	YSPRAIDMSN	VTLSRDLHAM	AEMMAENYHN
IWAKKKKMEL	ESKGGGNHPL	LVPYDTLTAK	EKAKDREKAQ	DILKFLQING
YAVSRGFKDL	ELDTPSIEKR	FAYSFLQQLI	RYVDEAHQYI	LEFDGGSRGK
GEHFPYEQEI	KFFAKVVLPL	IDQYFKNHRL	YFLSAASRPL	CSGGHASNKE
KEMVTSLFCK	LGVLVRHRIS	LFGNDATSIV	NCLHILGQTL	DARTVMKTGL
ESVKSALRAF	LDNAAEDLEK	TMENLKQGQF	THTRNQPKGV	TQIINYTTVA
LLPMLSSLFE	HIGQHQFGED	LILEDVQVSC	YRILTSLYAL	GTSKSIYVER
QRSALGECLA	AFAGAFPVAF	LETHLDKHNI	YSIYNTKSSR	ERAALSLPTN
VEDVCPNIPS	LEKLMEEIVE	LAESGIRYTQ	MPHVMEVILP	MLCSYMSRWW
EHGPENNPER	AEMCCTALNS	EHMNTLLGNI	LKIIYNNLGI	DEGAWMKRLA
VFSQPIINKV	KPQLLKTHFL	PLMEKLKKKA	ATVVSEEDHL	KAEARGDMSE
AELLILDEFT	TLARDLYAFY	PLLIRFVDYN	RAKWLKEPNP	EAEELFRMVA
EVFIYWSKSH	NFKREEQNFV	VQNEINNMSF	LITDTKSKMS	KAAVSDQERK
KMKRKGDRYS	MQTSLIVAAL	KRLLPIGLNI	CAPGDQELIA	LAKNRFSLKD
TEDEVRDIIR	SNIHLQGKLE	DPAIRWQMAL	YKDLPNRTDD	TSDPEKTVER
VLDIANVLFH	LEQKSKRVGR	RHYCLVEHPQ	RSKKAVWHKL	LSKQRKRAVV
ACFRMAPLYN	LPRHRAVNLF	LQGYEKSWIE	TEEHYFEDKL	IEDLAKPGAE
PPEEDEGTKR	VDPLHQLILL	FSRTALTEKC	KLEEDFLYMA	YADIMAKSCH
DEEDDDGEEE	VKSFEEKEME	KQKLLYQQAR	LHDRGAAEMV	LQTISASKGE
TGPMVAATLK	LGIAILNGGN	STVQQKMLDY	LKEKKDVGFF	QSLAGLMQSC
SVLDLNAFER	QNKAEGLGMV	TEEGSGEKVL	QDDEFTCDLF	RFLQLLCEGH
NSDFQNYLRT	QTGNNTTVNI	IISTVDYLLR	VQESISDFYW	YYSGKDVIDE
QGQRNFSKAI	QVAKQVFNTL	TEYIQGPCTG	NQQSLAHSRL	WDAVVGFLHV
FAHMQMKLSQ	DSSQIELLKE	LMDLQKDMVV	MLLSMLEGNV	VNGTIGKQMV
DMLVESSNNV	EMILKFFDMF	LKLKDLTSSD	TFKEYDPDGK	GVISKRDFHK
AMESHKHYTQ	SETEFLLSCA	ETDENETLDY	EEFVKRFHEP	AKDIGFNVAV
LLTNLSEHMP	NDTRLQTFLE	LAESVLNYFQ	PFLGRIEIMG	SAKRIERVYF
EISESSRTQW	EKPQVKESKR	QFIFDVVNEG	GEKEKMELFV	NFCEDTIFEM
QLAAQISESD	LNERSANKEE	SEKERPEEQG	PRMAFFSILT	VRSALFALRY
NILTLMRMLS	LKSLKKQMKK	VKKMTVKDMV	TAFFSSYWSI	FMTLLHFVAS
VFRGFFRIIC	SLLLGGSLVE	GAKKIKVAEL	LANMPDPTQD	EVRGDGEEGE
RKPLEAALPS	EDLTDLKELT	EESDLLSDIF	GLDLKREGGQ	YKLIPHNPNA
GLSDLMSNPV	PMPEVQEKFQ	EQKAKEEEKE	EKEETKSEPE	KAEGEDGEKE
EKAKEDKGKQ	KLRQLHTHRY	GEPEVPESAF	WKKIIAYQQK	LLNYFARNFY
NMRMLALFVA	FAINFILLFY	KVSTSSVVEG	KELPTRSSSE	NAKVTSLDSS
SHRIIAVHYV	LEESSGYMEP	TLRILAILHT	VISFFCIIGY	YCLKVPLVIF
KREKEVARKL	EFDGLYITEQ	PSEDDIKGQW	DRLVINTQSF	PNNYWDKFVK
RKVMDKYGEF	YGRDRISELL	GMDKAALDFS	DAREKKKPKK	DSSLSAVLNS
IDVKYQMWKL	GVVFTDNSFL	YLAWYMTMSV	LGHYNNFFFA	AHLLDIAMGF
KTLRTILSSV	THNGKQLVLT	VGLLAVVVYL	YTVVAFNFFR	KFYNKSEDGD
TPDMKCDDML	TCYMFHMYVG	VRAGGGIGDE	IEDPAGDEYE	IYRIIFDITF
FFFVIVILLA	IIQGLIIDAF	GELRDQQEQV	KEDMETKCFI	CGIGNDYFDT
VPHGFETHTL	QEHNLANYLF	FLMYLINKDE	TEHTGQESYV	WKMYQERCWE
FFPAGDCFRK	QYEDQLN

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

Funkcija

Protein RYR2 funkcionira kao glavna komponenta kalcijevog kanala u sarkoplazmatskom retikulumu koji opskrbljuje srčani mišić ionima tokom sistola. Da bi omogućio kontrakciju srčanog mišića, kalcijev priliv kroz naponski ograničeni L-tip kalcijskog kanala u plazemsmembrani omogućava da se ioni kalcija vežu za RYR2, koji se nalazi na sarkoplazmatskom retikulumu. Ovo vezanje uzrokuje oslobađanje kalcija kroz RYR2 iz sarkoplazmatskog retikuluma u citosol, gdje se veže za C domen troponina, koji pomiče tropomiozin i omogućava miozinskim ATPazama da se vežu za aktin, omogućavajući kontrakciju srčanog mišića.^[9] RYR2 kanali povezani su s mnogim ćelijskim funkcijama, uključujući metabolizam mitohondrija, ekspresiju gena i preživljavanje ćelija, pored njihove uloge u kontrakciji kardiomiocita.^[10]

Klinički značaj

Štetne mutacije porodice receptora za rijanodine, a posebno receptora RYR2, dovode do patoloških konstelacija koje dovode i do akutne i do hronične srčane insuficijencije, opće poznatih kao rijanopatije.^[11]

Mutacije u genu RYR2 povezane su sa kateholaminergijske polimorfna komorsksna tahikardija i aritmogena displazija desne komore.^[12]

Nedavno je iznenadna srčana smrt kod nekoliko mladih osoba u zajednici Amiša (od kojih su četiri iz iste porodice) pronađeno homozigotno umnožavanje mutantnog gena RyR2.^[13] Normalni (divlji tip) RyR2 funkcionira prvenstveno u srčanom mišiću.

Miševi s genetički reduciranim RYR2 pokazuju niži bazni puls i fatalne aritmije.^[14]

Interakcije

Pokazano je da receptor za riijanodin 2 ima interakcije sa:

Također pogledajte

Rijanodinski receptor

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000198626 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021313 - Ensembl, maj 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.
^ 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): 13472–83. doi:10.1016/S0021-9258(18)77371-7. PMID 2380170.
^ Otsu K, Fujii J, Periasamy M, Difilippantonio M, Uppender M, Ward DC, MacLennan DH (august 1993). "Chromosome mapping of five human cardiac and skeletal muscle sarcoplasmic reticulum protein genes". Genomics. 17 (2): 507–9. doi:10.1006/geno.1993.1357. PMID 8406504.
^ Tiso N, Stephan DA, Nava A, Bagattin A, Devaney JM, Stanchi F, et al. (februar 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): 189–94. doi:10.1093/hmg/10.3.189. PMID 11159936.
^ Guo T, Cornea RL, Huke S, Camors E, Yang Y, Picht E, et al. (juni 2010). "Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks". Circulation Research. 106 (11): 1743–52. doi:10.1161/CIRCRESAHA.110.219816. PMC 2895429. PMID 20431056.
^ "Q92736 - RYR2_HUMAN".
^ Bround MJ, Wambolt R, Luciani DS, Kulpa JE, Rodrigues B, Brownsey RW, et al. (juni 2013). "Cardiomyocyte ATP production, metabolic flexibility, and survival require calcium flux through cardiac ryanodine receptors in vivo". The Journal of Biological Chemistry. 288 (26): 18975–86. doi:10.1074/jbc.M112.427062. PMC 3696672. PMID 23678000.
^ Belevych AE, Radwański PB, Carnes CA, Györke S (maj 2013). "'Ryanopathy': causes and manifestations of RyR2 dysfunction in heart failure". Cardiovascular Research. 98 (2): 240–7. doi:10.1093/cvr/cvt024. PMC 3633158. PMID 23408344.
^ "Entrez Gene: RYR2 ryanodine receptor 2 (cardiac)".
^ Tester DJ, Bombei HM, Fitzgerald KK, Giudicessi JR, Pitel BA, Thorland EC, et al. (januar 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.
^ Bround MJ, Asghari P, Wambolt RB, Bohunek L, Smits C, Philit M, et al. (decembar 2012). "Cardiac ryanodine receptors control heart rate and rhythmicity in adult mice". Cardiovascular Research. 96 (3): 372–80. doi:10.1093/cvr/cvs260. PMC 3500041. PMID 22869620.
^ ^a ^b ^c ^d Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks AR (maj 2000). "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts". Cell. 101 (4): 365–76. doi:10.1016/S0092-8674(00)80847-8. PMID 10830164. S2CID 6496567.
^ Marx SO, Reiken S, Hisamatsu Y, Gaburjakova M, Gaburjakova J, Yang YM, et al. (maj 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.
^ Meyers MB, Pickel VM, Sheu SS, Sharma VK, Scotto KW, Fishman GI (novembar 1995). "Association of sorcin with the cardiac ryanodine receptor". The Journal of Biological Chemistry. 270 (44): 26411–8. doi:10.1074/jbc.270.44.26411. PMID 7592856.

Dopunska literatura

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Marks AR, Priori S, Memmi M, Kontula K, Laitinen PJ (januar 2002). "Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia". Journal of Cellular Physiology. 190 (1): 1–6. doi:10.1002/jcp.10031. PMID 11807805.
Marks AR (april 2002). "Ryanodine receptors, FKBP12, and heart failure". Frontiers in Bioscience. 7 (1–3): d970-7. doi:10.2741/marks. PMID 11897558.
Danieli GA, Rampazzo A (maj 2002). "Genetics of arrhythmogenic right ventricular cardiomyopathy". Current Opinion in Cardiology. 17 (3): 218–21. doi:10.1097/00001573-200205000-00002. PMID 12015469.
Ma J, Hayek SM, Bhat MB (2005). "Membrane topology and membrane retention of the ryanodine receptor calcium release channel". Cell Biochemistry and Biophysics. 40 (2): 207–24. doi:10.1385/CBB:40:2:207. PMID 15054223. S2CID 25375622.
Meyers MB, Pickel VM, Sheu SS, Sharma VK, Scotto KW, Fishman GI (novembar 1995). "Association of sorcin with the cardiac ryanodine receptor". The Journal of Biological Chemistry. 270 (44): 26411–8. doi:10.1074/jbc.270.44.26411. PMID 7592856.
Rampazzo A, Nava A, Erne P, Eberhard M, Vian E, Slomp P, et al. (novembar 1995). "A new locus for arrhythmogenic right ventricular cardiomyopathy (ARVD2) maps to chromosome 1q42-q43" (PDF). Human Molecular Genetics. 4 (11): 2151–4. doi:10.1093/hmg/4.11.2151. PMID 8589694.
Tunwell RE, Wickenden C, Bertrand BM, Shevchenko VI, Walsh MB, Allen PD, Lai FA (septembar 1996). "The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis". The Biochemical Journal. 318 (Pt 2): 477–87. doi:10.1042/bj3180477. PMC 1217646. PMID 8809036.
Awad SS, Lamb HK, Morgan JM, Dunlop W, Gillespie JI (mart 1997). "Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium". The Biochemical Journal. 322 (Pt 3): 777–83. doi:10.1042/bj3220777. PMC 1218255. PMID 9148749.
Martin C, Chapman KE, Seckl JR, Ashley RH (juli 1998). "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. doi:10.1016/S0306-4522(97)00612-X. PMID 9607712. S2CID 25634042.
Chambers P, Neal DE, Gillespie JI (januar 1999). "Ryanodine receptors in human bladder smooth muscle". Experimental Physiology. 84 (1): 41–6. doi:10.1111/j.1469-445x.1999.tb00070.x. PMID 10081705.
Mori F, Fukaya M, Abe H, Wakabayashi K, Watanabe M (maj 2000). "Developmental changes in expression of the three ryanodine receptor mRNAs in the mouse brain". Neuroscience Letters. 285 (1): 57–60. doi:10.1016/S0304-3940(00)01046-6. PMID 10788707. S2CID 32514035.
Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks AR (maj 2000). "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts". Cell. 101 (4): 365–76. doi:10.1016/S0092-8674(00)80847-8. PMID 10830164. S2CID 6496567.
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[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021313 - Ensembl, maj 2017

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