CoChat
Sign Up
Cited by 51Ion channel regulation and functionMuscle Physiology and DisordersCardiac electrophysiology and arrhythmias

Ion Channel Gene Mutations Causing Skeletal Muscle Disorders: Pathomechanisms and Opportunities for Therapy

Open access
Maggi, Lorenzo, Bonanno, Silvia, Altamura, Concetta, Desaphy, Jean-François·2021·Cells
DOI 10.3390/cells10061521PMC PMC8234207
Open this paper in CoChat — free accountOpen PDF

Abstract

Skeletal muscle ion channelopathies (SMICs) are a large heterogeneous group of rare genetic disorders caused by mutations in genes encoding ion channel subunits in the skeletal muscle mainly characterized by myotonia or periodic paralysis, potentially resulting in long-term disabilities. However, with the development of new molecular technologies, new genes and new phenotypes, including progressive myopathies, have been recently discovered, markedly increasing the complexity in the field. In this regard, new advances in SMICs show a less conventional role of ion channels in muscle cell division, proliferation, differentiation, and survival. Hence, SMICs represent an expanding and exciting field. Here, we review current knowledge of SMICs, with a description of their clinical phenotypes, cellular and molecular pathomechanisms, and available treatments.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/cells10061521

Cites

5 of 5 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • T3 activates wild-type Kir2.6 channels in healthy muscle to preserve the resting membrane potential and counteract T3-induced weakening.

    “Research suggests that triiodothyronine (T3) activates wild-type Kir2.6 channels in healthy muscle to preserve the resting membrane potential (RMP) and counteract T3-induced weakening [25].”

    From Thyrotoxic Hypokalemic Periodic Paralysis: Pathophysiological Mechanisms (2025) · cites this paper as [25]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 265

  1. [1]Fontaine B. Khurana T.S. Hoffman E.P. Bruns G.A. Haines J.L. Trofatter J.A. Hanson M.P. Rich J. McFarlane H. Yasek D.M. Hyperkalemic periodic paralysis and the adult muscle sodium channel alpha-subunit gene Science 1990 250 1000 1002 10.1126/science.2173143 2173143 · DOI
  2. [2]Horga A. Rayan D.L. Matthews E. Sud R. Fialho D. Durran S.C. Burge J.A. Portaro S. Davis M.B. Haworth A. Prevalence study of genetically defined skeletal muscle channelopathies in England Neurology 2013 80 1472 1475 10.1212/WNL.0b013e31828cf8d0 23516313 PMC3662361 · DOI
  3. [3]Stunnenberg B.C. Raaphorst J. Deenen J.C. Links T.P. Wilde A.A. Verbove D.J. Kamsteeg E.J. van den Wijngaard A. Faber C.G. van der Wilt G.J. Prevalence and mutation spectrum of skeletal muscle channelopathies in the Netherlands Neuromuscul. Disord. 2018 28 402 407 10.1016/j.nmd.2018.03.006 29606556 · DOI
  4. [4]Maggi L. Brugnoni R. Canioni E. Tonin P. Saletti V. Patrizia S. Cotti Piccinelli S. Colleoni L. Ferrigno P. Antonella P. Clinical and Molecular Spectrum of Myotonia and Periodic Paralyses Associated With Mutations in SCN4A in a Large Cohort of Italian Patients Front. Neurol. 2020 11 646 10.3389/fneur.2020.00646 32849172 PMC7403394 · DOI
  5. [5]Ptáček L.J. George A.L. Jr. Griggs R.C. Tawil R. Kallen R.G. Barchi R.L. Robertson M. Leppert M.F. Identification of a mutation in the gene causing hyperkalemic periodic paralysis Cell 1991 67 1021 1027 10.1016/0092-8674(91)90374-8 1659948 · DOI
  6. [6]Rojas C.V. Wang J.Z. Schwartz L.S. Hoffman E.P. Powell B.R. Brown R.H. Jr. A Met-to-Val mutation in the skeletal muscle Nav channel alpha-subunit in hyperkalaemic periodic paralysis Nature 1991 354 387 389 10.1038/354387a0 1659668 · DOI
  7. [7]Miller T.M. Da Silva M.D. Miller H.A. Kwiecinski H. Mendell J.R. Tawil R. McManis P. Griggs R.C. Angelini C. Servidei S. Correlating phenotype and genotype in the periodic paralyses Neurology 2004 63 1647 1655 10.1212/01.WNL.0000143383.91137.00 15534250 · DOI
  8. [8]Ptáček L.J. George A.L. Jr. Barchi R.L. Griggs R.C. Riggs J.E. Robertson M. Leppert M.F. Mutations in an S4 segment of the adult skeletal muscle sodium channel cause paramyotonia congenita Neuron 1992 8 891 897 10.1016/0896-6273(92)90203-P 1316765 · DOI
  9. [9]Matthews E. Fialho D. Tan S.V. Venance S.L. Cannon S.C. Sternberg D. Fontaine B. Amato A.A. Barohn R.J. Griggs R.C. The non-dystrophic myotonias: Molecular pathogenesis, diagnosis and treatment Brain 2010 133 9 22 10.1093/brain/awp294 19917643 PMC2801326 · DOI
  10. [10]Lerche H. Heine R. Pika U. George Jr A.L. Mitrovic N. Browatzki M. Weiss T. Rivet-Bastide M. Franke C. Lomonaco M. Human sodium channel myotonia: Slowed channel inactivation due to substitutions for a glycine within the III-IV linker J. Physiol. 1993 470 13 22 10.1113/jphysiol.1993.sp019843 8308722 PMC1143902 · DOI
  11. [11]Trip J. Drost G. Ginjaar H.B. Nieman F.H. van der Kooi A.J. de Visser M. van Engelen B.G. Faber C.G. Redefining the clinical phenotypes of non-dystrophic myotonic syndromes J. Neurol. Neurosurg. Psychiatry 2009 80 647 652 10.1136/jnnp.2008.162396 19211598 · DOI
  12. [12]Cea G. Andreu D. Fletcher E. Ramdas S. Sud R. Hanna M.G. Matthews E. Sodium channel myotonia may be associated with high-risk brief resolved unexplained events Wellcome Open Res. 2020 5 57 10.12688/wellcomeopenres.15798.2 32509969 PMC7241273 · DOI
  13. [13]Fusco C. Frattini D. Salerno G.G. Canali E. Bernasconi P. Maggi L. New phenotype and neonatal onset of sodium channel myotonia in a child with a novel mutation of SCN4A gene Brain Dev. 2015 37 891 893 10.1016/j.braindev.2015.02.004 25735906 · DOI
  14. [14]Bednarz M. Stunnenberg B.C. Kusters B. Kamsteeg E.J. Saris C.G. Groome J. Winston V. Meola G. Jurkat-Rott K. Voermans N.C. A novel Ile1455Thr variant in the skeletal muscle sodium channel alpha-subunit in a patient with a severe adult-onset proximal myopathy with electrical myotonia and a patient with mild paramyotonia phenotype Neuromuscul. Disord. 2017 27 175 182 10.1016/j.nmd.2016.09.023 28024841 · DOI
  15. [15]Luo S. Castañeda M.S. Matthews E. Sud R. Hanna M.G. Sun J. Song J. Lu J. Qiao K. Zhao C. Hypokalaemic periodic paralysis and myotonia in a patient with homozygous mutation p.R1451L in Nav1.4 Sci. Rep. 2018 8 9714 10.1038/s41598-018-27822-2 29946067 PMC6018793 · DOI
  16. [16]Elia N. Nault T. McMillan H.J. Graham G.E. Huang L. Cannon S.C. Myotonic myopathy with secondary joint and skeletal anomalies from the c.2386C>G, p.L769V mutation in SCN4A Front. Neurol. 2020 11 77 10.3389/fneur.2020.00077 32117035 PMC7031655 · DOI
  17. [17]Poulin H. Gosselin-Badaroudine P. Vicart S. Habbout K. Sternberg D. Giuliano S. Fontaine B. Bendahhou S. Nicole S. Chahine M. Substitutions of the S4DIV R2 residue (R1451) in NaV1.4 lead to complex forms of paramyotonia congenita and periodic paralyses Sci. Rep. 2018 8 2041 10.1038/s41598-018-20468-0 29391559 PMC5794747 · DOI
  18. [18]Taminato T. Mori-Yoshimura M. Miki J. Sasaki R. Sato N. Oya Y. Nishino I. Takahashi Y. Paramyotonia Congenita with Persistent Distal and Facial Muscle Weakness: A Case Report with Literature Review J. Neuromuscul. Dis. 2020 7 193 201 10.3233/JND-190440 32083589 · DOI
  19. [19]Cannon S.C. Sodium channelopathies of skeletal muscle Handb. Exp. Pharmacol. 2018 246 309 330 28939973 PMC5866235
  20. [20]Cannon S.C. Brown R.H. Jr. Corey D.P. Theoretical reconstruction of myotonia and paralysis caused by incomplete inactivation of sodium channels Biophys. J. 1993 65 270 288 10.1016/S0006-3495(93)81045-2 8396455 PMC1225722 · DOI
  21. [21]Hayward L.J. Sandoval G.M. Cannon S.C. Defective slow inactivation of sodium channels contributes to familial periodic paralysis Neurology 1999 52 1447 1453 10.1212/WNL.52.7.1447 10227633 · DOI
  22. [22]Statland J.M. Bundy B.N. Wang Y. Rayan D.R. Trivedi J.R. Sansone V.A. Salajegheh M.K. Venance S.L. Ciafaloni E. Matthews E. Mexiletine for symptoms and signs of myotonia in nondystrophic myotonia: A randomized controlled trial JAMA 2012 308 1357 1365 10.1001/jama.2012.12607 23032552 PMC3564227 · DOI
  23. [23]Stunnenberg B.C. Raaphorst J. Groenewoud H.M. Statland J.M. Griggs R.C. Woertman W. Stegeman D.F. Timmermans J. Trivedi J. Matthews E. Effect of mexiletine on muscle stiffness in patients with nondystrophic myotonia evaluated using aggregated N-of-1 trials JAMA 2018 320 2344 2353 10.1001/jama.2018.18020 30535218 PMC6583079 · DOI
  24. [24]Suetterlin K.J. Bugiardini E. Kaski J.P. Morrow J.M. Matthews E. Hanna M.G. Fialho D. Long-term safety and efficacy of mexiletine for patients with skeletal muscle channelopathies JAMA Neurol. 2015 72 1531 1533 10.1001/jamaneurol.2015.2338 26658970 · DOI
  25. [25]Modoni A. D’Amico A. Primiano G. Capozzoli F. Desaphy J.-F. Lo Monaco M. Long-term safety and usefulness of mexiletine in a large cohort of patients affected by non-dystrophic myotonias Front. Neurol. 2020 11 300 10.3389/fneur.2020.00300 32655465 PMC7326038 · DOI
  26. [26]Andersen G. Hedermann G. Witting N. Duno M. Andersen H. Vissing J. The antimyotonic effect of lamotrigine in non-dystrophic myotonias: A double-blind randomized study Brain 2017 140 2295 2305 10.1093/brain/awx192 29050397 · DOI
  27. [27]Vereb N. Montagnese F. Gläser D. Schoser B. Non-dystrophic myotonias: Clinical and mutation spectrum of 70 German patients J. Neurol. 2021 268 1708 1720 10.1007/s00415-020-10328-1 33263785 PMC8068660 · DOI
  28. [28]Desaphy J.F. Modoni A. Lomonaco M. Camerino D.C. Dramatic improvement of myotonia permanens with flecainide: A two-case report of a possible bench-to-bedside pharmacogenetics strategy Eur. J. Clin. Pharmacol. 2013 69 1037 1039 10.1007/s00228-012-1414-3 23052413 PMC3621996 · DOI
  29. [29]Desaphy J.F. Carbonara R. D’Amico A. Modoni A. Roussel J. Imbrici P. Pagliarani S. Lucchiari S. Lo Monaco M. Conte Camerino D. Translational approach to address therapy in myotonia permanens due to a new SCN4A mutation Neurology 2016 86 2100 2108 10.1212/WNL.0000000000002721 27164696 PMC4891212 · DOI
  30. [30]Farinato A. Altamura C. Imbrici P. Maggi L. Bernasconi P. Mantegazza R. Pasquali L. Siciliano G. Monaco M.L. Vial C. Pharmacogenetics of myotonic hNav1.4 sodium channel variants situated near the fast inactivation gate Pharmacol. Res. 2019 141 224 235 10.1016/j.phrs.2019.01.004 30611854 · DOI
  31. [31]Desaphy J.F. Altamura C. Vicart S. Fontaine B. Targeted Therapies for Skeletal Muscle Ion Channelopathies: Systematic Review and Steps Towards Precision Medicine J. Neuromuscul. Dis. 2021 8 357 381 10.3233/JND-200582 33325393 PMC8203248 · DOI
  32. [32]Desaphy J.F. Carbonara R. Costanza T. Conte Camerino D. Preclinical evaluation of marketed sodium channel blockers in a rat model of myotonia discloses promising antimyotonic drugs Exp. Neurol. 2014 255 96 102 10.1016/j.expneurol.2014.02.023 24613829 PMC4004800 · DOI
  33. [33]Desaphy J.F. Farinato A. Altamura C. De Bellis M. Imbrici P. Tarantino N. Caccia C. Melloni E. Padoani G. Vailati S. Safinamide’s potential in treating nondystrophic myotonias: Inhibition of skeletal muscle voltage-gated sodium channels and skeletal muscle hyperexcitability in vitro and in vivo Exp. Neurol. 2020 328 113287 10.1016/j.expneurol.2020.113287 32205118 · DOI
  34. [34]Novak K.R. Norman J. Mitchell J.R. Pinter M.J. Rich M.M. Sodium channel slow inactivation as a therapeutic target for myotonia congenita Ann. Neurol. 2015 77 320 332 10.1002/ana.24331 25515836 PMC4315705 · DOI
  35. [35]Skov M. de Paoli F.V. Nielsen O.B. Pedersen T.H. The anti-convulsants lacosamide, lamotrigine, and rufinamide reduce myotonia in isolated human and rat skeletal muscle Muscle Nerve 2017 56 136 142 10.1002/mus.25452 27783415 · DOI
  36. [36]De Bellis M. Carbonara R. Roussel J. Farinato A. Massari A. Pierno S. Muraglia M. Corbo F. Franchini C. Carratù M.R. Increased sodium channel use-dependent inhibition by a new potent analogue of tocainide greatly enhances in vivo antimyotonic activity Neuropharmacology 2017 113 206 216 10.1016/j.neuropharm.2016.10.013 27743929 PMC5154332 · DOI
  37. [37]De Bellis M. De Luca A. Desaphy J.F. Carbonara R. Heiny J.A. Kennedy A. Carocci A. Cavalluzzi M.M. Lentini G. Franchini C. Combined modifications of mexiletine pharmacophores for new lead blockers of Na(v)1.4 channels Biophys. J. 2013 104 344 354 10.1016/j.bpj.2012.11.3830 23442856 PMC3552273 · DOI
  38. [38]Tricarico D. Mele A. Conte Camerino D. Carbonic anhydrase inhibitors ameliorate the symptoms of hypokalaemic periodic paralysis in rats by opening the muscular Ca2+- activated-K+channels Neuromuscul. Disord. 2006 16 39 45 10.1016/j.nmd.2005.10.005 16368240 · DOI
  39. [39]Altamura C. Fonzino A. Tarantino N. Conte E. Liantonio A. Imbrici P. Carratù M.R. Pierno S. Desaphy J.F. Increased sarcolemma chloride conductance as one of the mechanisms of action of carbonic anhydrase inhibitors in muscle excitability disorders Exp. Neurol. 2021 342 113758 10.1016/j.expneurol.2021.113758 33991525 · DOI
  40. [40]Sansone V.A. Burge J. McDermott M.P. Smith P.C. Herr B. Tawil R. Pandya S. Kissel J. Ciafaloni E. Shieh P. Randomized, placebo-controlled trials of dichlorphenamide in periodic paralysis Neurology 2016 86 1408 1416 10.1212/WNL.0000000000002416 26865514 PMC4831040 · DOI
  41. [41]Statland J.M. Fontaine B. Hanna M.G. Johnson N.E. Kissel J.T. Sansone V.A. Shieh P.B. Tawil R.N. Trivedi J. Cannon S.C. Review of the Diagnosis and Treatment of Periodic Paralysis Muscle Nerve 2018 57 522 530 10.1002/mus.26009 29125635 PMC5867231 · DOI
  42. [42]Stunnenberg B.C. LoRusso S. Arnold W.D. Barohn R.J. Cannon S.C. Fontaine B. Griggs R.C. Hanna M.G. Matthews E. Meola G. Guidelines on clinical presentation and management of nondystrophic myotonias Muscle Nerve 2020 62 430 444 10.1002/mus.26887 32270509 PMC8117169 · DOI
  43. [43]Bulman D.E. Scoggan K.A. van Oene M.D. Nicolle M.W. Hahn A.F. Tollar L.L. Ebers G.C. A novel sodium channel mutation in a family with hypokalemic periodic paralysis Neurology 1999 53 1932 1936 10.1212/WNL.53.9.1932 10599760 · DOI
  44. [44]Jurkat-Rott K. Mitrovic N. Hang C. Kouzmenkine A. Iaizzo P. Herzog J. Lerche H. Nicole S. Vale-Santos J. Chauveau D. Voltage-sensor sodium channel mutations cause hypokalemic periodic paralysis type 2 by enhanced inactivation and reduced current Proc. Natl. Acad. Sci. USA 2000 97 9549 9554 10.1073/pnas.97.17.9549 10944223 PMC16902 · DOI
  45. [46]Matthews E. Portaro S. Ke Q. Sud R. Haworth A. Davis M.B. Griggs R.C. Hanna M.G. ACZ efficacy in hypokalemic periodic paralysis and the predictive role of genotype Neurology 2011 77 1960 1964 10.1212/WNL.0b013e31823a0cb6 22094484 PMC3235354 · DOI
  46. [47]Tsujino A. Maertens C. Ohno K. Shen X.M. Fukuda T. Harper C.M. Cannon S.C. Engel A.G. Myasthenic syndrome caused by mutation of the SCN4A sodium channel Proc. Natl. Acad. Sci. USA 2003 100 7377 7382 10.1073/pnas.1230273100 12766226 PMC165883 · DOI
  47. [48]Zaharieva I.T. Thor M.G. Oates E.C. Van Karnebeek C. Hendson G. Blom E. Witting N. Rasmussen M. Gabbett M.T. Ravenscroft G. Loss-of-function mutations in SCN4A cause severe foetal hypokinesia or classical congenital myopathy Brain 2016 139 674 691 10.1093/brain/awv352 26700687 PMC4766374 · DOI
  48. [49]Thompson R. Bonne G. Missier P. Lochmüller H. Targeted therapies for congenital myasthenic syndromes: Systematic review and steps towards a treatabolome Emerg. Top. Life Sci. 2019 3 19 37 30931400 PMC6436731
  49. [50]Matthews E. Hartley L. Sud R. Hanna M.G. Muntoni F. Munot P. Acetazolamide can improve symptoms and signs in ion channel-related congenital myopathy J. Neurol. Neurosurg. Psychiatry 2019 90 243 245 10.1136/jnnp-2017-317849 29769250 · DOI
  50. [51]Ptáček L.J. Tawil R. Griggs R.C. Engel A.G. Layzer R.B. Kwieciński H. McManis P.G. Santiago L. Moore M. Fouad G. Dihydropyridine receptor mutations cause hypokalemic periodic paralysis Cell 1994 77 863 868 10.1016/0092-8674(94)90135-X 8004673 · DOI
  51. [52]Holm-Yildiz S. Witting N. Dahlqvist J. de Stricker Borch J. Solheim T. Fornander F. Eisum A.S. Duno M. Soerensen T. Vissing J. Permanent muscle weakness in hypokalemic periodic paralysis Neurology 2020 95 e342 e352 10.1212/WNL.0000000000009828 32580975 · DOI
  52. [53]Fan C. Lehmann-Horn F. Weber M.A. Bednarz M. Groome J.R. Jonsson M.K. Transient compartment-like syndrome and normokalaemic periodic paralysis due to a Ca(v)1.1 mutation Brain 2013 136 3775 3786 10.1093/brain/awt300 24240197 PMC3859226 · DOI
  53. [54]Wu F. Mi W. Hernández-Ochoa E.O. Burns D.K. Fu Y. Gray H.F. Struyk A.F. Schneider M.F. Cannon S.C. A calcium channel mutant mouse model of hypokalemic periodic paralysis J. Clin. Investig. 2012 122 4580 4591 10.1172/JCI66091 23187123 PMC3533564 · DOI
  54. [55]Schartner V. Romero N.B. Donkervoort S. Treves S. Munot P. Pierson T.M. Dabaj I. Malfatti E. Zaharieva I.T. Zorzato F. Dihydropyridine receptor (DHPR, CACNA1S) congenital myopathy Acta Neuropathol. 2017 133 517 533 10.1007/s00401-016-1656-8 28012042 · DOI
  55. [56]Jungbluth H. Treves S. Zorzato F. Sarkozy A. Ochala J. Sewry C. Phadke R. Gautel M. Muntoni F. Congenital myopathies: Disorders of excitation-contraction coupling and muscle contraction Nat. Rev. Neurol. 2018 14 151 167 10.1038/nrneurol.2017.191 29391587 · DOI
  56. [57]Hunter J.M. Ahearn M.E. Balak C.D. Liang W.S. Kurdoglu A. Corneveaux J.J. Russell M. Huentelman M.J. Craig D.W. Carpten J. Novel pathogenic variants and genes for myopathies identified by whole exome sequencing Mol. Genet. Genomic Med. 2015 3 283 301 10.1002/mgg3.142 26247046 PMC4521965 · DOI
  57. [58]Ravenscroft G. Clayton J.S. Faiz F. Sivadorai P. Milnes D. Cincotta R. Moon P. Kamien B. Edwards M. Delatycki M. Neurogenetic fetal akinesia and arthrogryposis: Genetics, expanding genotype-phenotypes and functional genomics J. Med. Genet. 2020 10.1136/jmedgenet-2020-106901 PMC8328565 33060286 · DOI
  58. [59]Yiş U. Hiz S. Güneş S. Diniz G. Baydan F. Töpf A. Sonmezler E. Lochmüller H. Horvath R. Oktay Y. Dihydropyridine Receptor Congenital Myopathy In A Consangineous Turkish Family J. Neuromuscul. Dis. 2019 6 377 384 10.3233/JND-190383 31227654 PMC6736676 · DOI
  59. [60]Flucher B.E. Campiglio M. STAC proteins: The missing link in skeletal muscle EC coupling and new regulators of calcium channel function Biochim. Biophys. Acta Mol. Cell. Res. 2019 1866 1101 1110 10.1016/j.bbamcr.2018.12.004 30543836 · DOI
  60. [61]Nelson B.R. Wu F. Liu Y. Anderson D.M. McAnally J. Lin W. Cannon S.C. Bassel-Duby R. Olson E.N. Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility Proc. Natl. Acad. Sci. USA 2013 110 11881 11886 10.1073/pnas.1310571110 23818578 PMC3718085 · DOI
  61. [62]Horstick E.J. Linsley J.W. Dowling J.J. Hauser M.A. McDonald K.K. Ashley-Koch A. Saint-Amant L. Satish A. Cui W.W. Zhou W. Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy Nat. Commun. 2013 4 1952 10.1038/ncomms2952 23736855 PMC4056023 · DOI
  62. [63]Bailey A.G. Bloch E.C. Malignant hyperthermia in a three-month-old American Indian infant Anesth. Analg. 1987 66 1043 1045 10.1213/00000539-198710000-00028 3631569 · DOI
  63. [64]Stewart C.R. Kahler S.G. Gilchrist J.M. Congenital myopathy with cleft palate and increased susceptibility to malignant hyperthermia: King syndrome? Pediatr. Neurol. 1988 4 371 374 10.1016/0887-8994(88)90086-0 3245876 · DOI
  64. [65]Stamm D.S. Aylsworth A.S. Stajich J.M. Kahler S.G. Thorne L.B. Speer M.C. Powell C.M. Native American myopathy: Congenital myopathy with cleft palate, skeletal anomalies, and susceptibility to malignant hyperthermia Am. J. Med. Genet. A 2008 146 1832 1841 10.1002/ajmg.a.32370 18553514 · DOI
  65. [66]Flucher B.E. Skeletal muscle Cav1.1 channelopathies Pflug. Arch. 2020 472 739 754 10.1007/s00424-020-02368-3 32222817 PMC7351834 · DOI
  66. [67]Telegrafi A. Webb B.D. Robbins S.M. Speck-Martins C.E. FitzPatrick D. Fleming L. Redett R. Dufke A. Houge G. van Harssel J.J. Identification of STAC3 variants in non-Native American families with overlapping features of Carey-Fineman-Ziter syndrome and Moebius syndrome Am. J. Med. Genet. A 2017 173 2763 2771 10.1002/ajmg.a.38375 28777491 PMC5843189 · DOI
  67. [68]Zaharieva I.T. Sarkozy A. Munot P. Manzur A. O’Grady G. Rendu J. Malfatti E. Amthor H. Servais L. Urtizberea J.A. STAC3 variants cause a congenital myopathy with distinctive dysmorphic features and malignant hyperthermia susceptibility Hum. Mutat. 2018 39 1980 1994 10.1002/humu.23635 30168660 · DOI
  68. [69]Grzybowski M. Schänzer A. Pepler A. Heller C. Neubauer B.A. Hahn A. Novel STAC3 Mutations in the First Non-Amerindian Patient with Native American Myopathy Neuropediatrics 2017 48 451 455 28411587
  69. [70]Wong King Yuen S.M. Campiglio M. Tung C.C. Flucher B.E. Van Petegem F. Structural insights into binding of STAC proteins to voltage-gated calcium channels Proc. Natl. Acad. Sci. USA 2017 114 E9520 E9528 10.1073/pnas.1708852114 29078335 PMC5692558 · DOI
  70. [71]Campiglio M. Kaplan M.M. Flucher B.E. STAC3 incorporation into skeletal muscle triads occurs independent of the dihydropyridine receptor J. Cell. Physiol. 2018 233 9045 9051 10.1002/jcp.26767 30071129 PMC6334165 · DOI
  71. [72]Hoth M. Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells Nature 1992 355 353 356 10.1038/355353a0 1309940 · DOI
  72. [73]Prakriya M. The molecular physiology of CRAC channels Immunol. Rev. 2009 231 88 98 10.1111/j.1600-065X.2009.00820.x 19754891 PMC3253762 · DOI
  73. [74]Lacruz R.S. Feske S. Diseases caused by mutations in ORAI1 and STIM1 Ann. N. Y. Acad. Sci. 2015 1356 45 79 10.1111/nyas.12938 26469693 PMC4692058 · DOI
  74. [75]Roos J. DiGregorio P.J. Yeromin A.V. Ohlsen K. Lioudyno M. Zhang S. Safrina O. Kozak J.A. Wagner S.L. Cahalan M.D. STIM1, an essential and conserved component of store-operated Ca2+ channel function J. Cell. Biol. 2005 169 435 445 10.1083/jcb.200502019 15866891 PMC2171946 · DOI
  75. [76]Vig M. Peinelt C. Beck A. Koomoa D.L. Rabah D. Koblan-Huberson M. Kraft S. Turner H. Fleig A. Penner R. CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry Science 2006 312 1220 1223 10.1126/science.1127883 16645049 PMC5685805 · DOI
  76. [77]González-Sánchez P. Del Arco A. Esteban J.A. Satrústegui J. Store-Operated Calcium Entry Is Required for mGluR-Dependent Long Term Depression in Cortical Neurons Front. Cell. Neurosci. 2017 11 363 10.3389/fncel.2017.00363 29311823 PMC5735122 · DOI
  77. [78]Lunz V. Romanin C. Frischauf I. STIM1 activation of Orai1 Cell Calcium 2019 77 29 38 10.1016/j.ceca.2018.11.009 30530091 PMC7617211 · DOI
  78. [79]Conte E. Pannunzio A. Imbrici P. Camerino G.M. Maggi L. Mora M. Gibertini S. Cappellari O. De Luca A. Coluccia M. Gain-of-Function STIM1 L96V Mutation Causes Myogenesis Alteration in Muscle Cells From a Patient Affected by Tubular Aggregate Myopathy Front. Cell. Dev. Biol. 2021 9 635063 10.3389/fcell.2021.635063 33718371 PMC7952532 · DOI
  79. [80]Feske S. Gwack Y. Prakriya M. Srikanth S. Puppel S.H. Tanasa B. Hogan P.G. Lewis R.S. Daly M. Rao A. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function Nature 2006 441 179 185 10.1038/nature04702 16582901 · DOI
  80. [81]Hou X. Pedi L. Diver M.M. Long S.B. Crystal structure of the calcium release-activated calcium channel Orai Science 2012 338 1308 1313 10.1126/science.1228757 23180775 PMC3695727 · DOI
  81. [82]Wang X. Wang Y. Zhou Y. Hendron E. Mancarella S. Andrake M.D. Rothberg B.S. Soboloff J. Gill D.L. Distinct Orai-coupling domains in STIM1 and STIM2 define the Orai-activating site Nat. Commun. 2014 5 3183 10.1038/ncomms4183 24492416 PMC3995141 · DOI
  82. [83]Schaballie H. Rodriguez R. Martin E. Moens L. Frans G. Lenoir C. Dutré J. Canioni D. Bossuyt X. Fischer A. A novel hypomorphic mutation in STIM1 results in a late-onset immunodeficiency J. Allergy Clin. Immunol. 2015 136 816 819 10.1016/j.jaci.2015.03.009 25935105 · DOI
  83. [84]Stormorken H. Sjaastad O. Langslet A. Sulg I. Egge K. Diderichsen J. A new syndrome: Thrombocytopathia, muscle fatigue, asplenia, miosis, migraine, dyslexia and ichthyosis Clin. Genet. 1985 28 67 74 10.1111/j.1399-0004.1985.tb02209.x 4085141 · DOI
  84. [85]Mizobuchi M. Tanaka C. Sako K. Murakami N. Nihira A. Abe T. Tateno Y. Takahashi T. Nonaka I. Muscle involvement of Stormorken’s syndrome Rinsho Shinkeigaku 2000 40 915 920 11257789
  85. [86]Markello T. Chen D. Kwan J.Y. Horkayne-Szakaly I. Morrison A. Simakova O. Maric I. Lozier J. Cullinane A.R. Kilo T. York platelet syndrome is a CRAC channelopathy due to gain-of-function mutations in STIM1 Mol. Genet. Metab. 2015 114 474 482 10.1016/j.ymgme.2014.12.307 25577287 PMC4355183 · DOI
  86. [87]Cameron C.H.S. Allen I.V. Patterson V. Avaria M.A. Dominantly inherited tubular aggregate myopathy J. Pathol. 1992 168 397 403 10.1002/path.1711680410 1484321 · DOI
  87. [88]Engel W.K. Mitochondrial Aggregates In Muscle Disease J. Histochem. Cytochem. 1964 12 46 48 10.1177/12.1.46 14187309 · DOI
  88. [89]Nesin V. Wiley G. Kousi M. Ong E.C. Lehmann T. Nicholl D.J. Suri M. Shahrizaila N. Katsanis N. Gaffney P.M. Activating mutations in STIM1 and ORAI1 cause overlapping syndromes of tubular myopathy and congenital miosis Proc. Nat. Acad. Sci. USA 2014 111 4197 4202 10.1073/pnas.1312520111 24591628 PMC3964084 · DOI
  89. [90]Morin G. Bruechle N.O. Singh A.R. Knopp C. Jedraszak G. Elbracht M. Brémond-Gignac D. Hartmann K. Sevestre H. Deutz P. Gain-of-function mutation in STIM1 (P.R304W) is associated with Stormorken syndrome Hum. Mutat. 2014 35 1221 1232 10.1002/humu.22621 25044882 · DOI
  90. [91]Guergueltcheva V. Müller J.S. Dusl M. Senderek J. Oldfors A. Lindbergh C. Maxwell S. Colomer J. Mallebrera C.J. Nascimento A. Congenital myasthenic syndrome with tubular aggregates caused by GFPT1 mutations J. Neurol. 2012 259 838 850 10.1007/s00415-011-6262-z 21975507 · DOI
  91. [92]Belaya K. Finlayson S. Slater C.R. Cossins J. Liu W.W. Maxwell S. McGowan S.J. Maslau S. Twigg S.R. Walls T.J. Mutations in DPAGT1 cause a limb-girdle congenital myasthenic syndrome with tubular aggregates Am. J. Hum. Genet. 2012 91 193 201 10.1016/j.ajhg.2012.05.022 22742743 PMC3397259 · DOI
  92. [93]Sternberg D. Maisonobe T. Jurkat-Rott K. Nicole S. Launay E. Chauveau D. Tabti N. Lehmann-Horn F. Hainque B. Fontaine B. Hypokalaemic periodic paralysis type 2 caused by mutations at codon 672 in the muscle sodium channel gene SCN4A Brain 2001 124 1091 1099 10.1093/brain/124.6.1091 11353725 · DOI
  93. [94]Böhm J. Chevessier F. De Paula A.M. Koch C. Attarian S. Feger C. Hantaï D. Laforêt P. Ghorab K. Vallat J.M. Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy Am. J. Hum. Genet. 2013 92 271 278 10.1016/j.ajhg.2012.12.007 23332920 PMC3567276 · DOI
  94. [95]Böhm J. Chevessier F. Koch C. Peche G.A. Mora M. Morandi L. Pasanisi B. Moroni I. Tasca G. Fattori F. Clinical, histological and genetic characterisation of patients with tubular aggregate myopathy caused by mutations in STIM1 J. Med. Genet. 2014 51 824 833 10.1136/jmedgenet-2014-102623 25326555 · DOI
  95. [96]Hedberg C. Niceta M. Fattori F. Lindvall B. Ciolfi A. D’Amico A. Tasca G. Petrini S. Tulinius M. Tartaglia M. Childhood onset tubular aggregate myopathy associated with de novo STIM1 mutations J. Neurol. 2014 261 870 876 10.1007/s00415-014-7287-x 24570283 · DOI
  96. [97]Claeys T. Goosens V. Racé V. Theys T. Thal D.R. Depuydt C.E. Claeys K.G. Clinical and muscle MRI features in a family with tubular aggregate myopathy and novel STIM1 mutation Neuromuscul. Disord. 2020 30 709 718 10.1016/j.nmd.2020.07.010 32893083 · DOI
  97. [98]Silva-Rojas R. Laporte J. Böhm J. STIM1/ORAI1 Loss-of-Function and Gain-of-Function Mutations Inversely Impact on SOCE and Calcium Homeostasis and Cause Multi-Systemic Mirror Diseases Front. Physiol. 2020 11 604941 10.3389/fphys.2020.604941 33250786 PMC7672041 · DOI
  98. [99]Misceo D. Holmgren A. Louch W.E. Holme P.A. Mizobuchi M. Morales R.J. De Paula A.M. Stray-Pedersen A. Lyle R. Dalhus B. A dominant STIM1 mutation causes Stormorken syndrome Hum. Mutat. 2014 35 556 564 10.1002/humu.22544 24619930 · DOI
  99. [100]Endo Y. Noguchi S. Hara Y. Hayashi Y.K. Motomura K. Miyatake S. Murakami N. Tanaka S. Yamashita S. Kizu R. Dominant mutations in ORAI1 cause tubular aggregate myopathy with hypocalcemia via constitutive activation of store-operated Ca(2)(+) channels Hum. Mol. Genet. 2015 24 637 648 10.1093/hmg/ddu477 25227914 · DOI
  100. [101]Böhm J. Bulla M. Urquhart J.E. Malfatti E. Williams S.G. O’Sullivan J. Szlauer A. Koch C. Baranello G. Mora M. ORAI1 Mutations with Distinct Channel Gating Defects in Tubular Aggregate Myopathy Hum. Mutat. 2017 38 426 438 10.1002/humu.23172 28058752 · DOI
  101. [102]Garibaldi M. Fattori F. Riva B. Labasse C. Brochier G. Ottaviani P. Sacconi S. Vizzaccaro E. Laschena F. Romero N.B. A novel gain-of-function mutation in ORAI1 causes late-onset tubular aggregate myopathy and congenital miosis Clin. Genet. 2017 91 780 786 10.1111/cge.12888 27882542 · DOI
  102. [103]Stauderman K.A. CRAC channels as targets for drug discovery and development Cell. Calcium. 2018 74 147 159 10.1016/j.ceca.2018.07.005 30075400 · DOI
  103. [104]Phillips M.S. Fujii J. Khanna V.K. DeLeon S. Yokobata K. de Jong P.J. MacLennan D.H. The structural organization of the human skeletal muscle ryanodine receptor (RYR1) gene Genomics 1996 34 24 41 10.1006/geno.1996.0238 8661021 · DOI
  104. [105]Dowling J.J.D. Gonorazky H. Cohn R.D. Campbell C. Treating pediatric neuromuscular disorders: The future is now Am. J. Med. Genet. A 2018 176 804 841 10.1002/ajmg.a.38418 28889642 PMC5900978 · DOI
  105. [106]Klein A. Lillis S. Munteanu I. Scoto M. Zhou H. Quinlivan R. Straub V. Manzur A.Y. Roper H. Jeannet P.Y. Clinical and genetic findings in a large cohort of patients with ryanodine receptor 1 gene-associated myopathies Hum. Mutat. 2012 33 981 988 10.1002/humu.22056 22473935 · DOI
  106. [107]Dlamini N. Voermans N.C. Lillis S. Stewart K. Kamsteeg E.J. Drost G. Quinlivan R. Snoeck M. Norwood F. Radunovic A. Mutations in RYR1 are a common cause of exertional myalgia and rhabdomyolysis Neuromuscul. Disord. 2013 23 540 548 10.1016/j.nmd.2013.03.008 23628358 · DOI
  107. [108]Løseth S. Voermans N.C. Torbergsen T. Lillis S. Jonsrud C. Lindal S. Kamsteeg E.J. Lammens M. Broman M. Dekomien G. A novel late-onset axial myopathy associated with mutations in the skeletal muscle ryanodine receptor (RYR1) gene J. Neurol. 2013 260 1504 1510 10.1007/s00415-012-6817-7 23329375 · DOI
  108. [109]Zou Y. Liang Y. Gong H. Zhou N. Ma H. Guan A. Sun A. Wang P. Niu Y. Jiang H. Ryanodine receptor type 2 is required for the development of pressure overload-induced cardiac hypertrophy Hypertension 2011 58 1099 1110 10.1161/HYPERTENSIONAHA.111.173500 21986507 · DOI
  109. [110]Zhou H. Rokach O. Feng L. Munteanu I. Mamchaoui K. Wilmshurst J.M. Sewry C. Manzur A.Y. Pillay K. Mouly V. RyR1 deficiency in congenital myopathies disrupts excitation-contraction coupling Hum. Mutat. 2013 34 986 996 10.1002/humu.22326 23553787 · DOI
  110. [111]Garibaldi M. Rendu J. Brocard J. Lacene E. Fauré J. Brochier G. Beuvin M. Labasse C. Madelaine A. Malfatti E. Dusty core disease (DuCD): Expanding morphological spectrum of RYR1 recessive myopathies Acta Neuropathol. Commun. 2019 7 3 10.1186/s40478-018-0655-5 30611313 PMC6320585 · DOI
  111. [112]Matthews E. Neuwirth C. Jaffer F. Scalco R.S. Fialho D. Parton M. Rayan D.R. Suetterlin K. Sud R. Spiegel R. Atypical periodic paralysis and myalgia: A novel RYR1 phenotype Neurology 2018 90 e412 e418 10.1212/WNL.0000000000004894 29298851 PMC5791790 · DOI
  112. [113]Lawal T.A. Todd J.J. Witherspoon J.W. Bönnemann C.G. Dowling J.J. Hamilton S.L. Meilleur K.G. Dirksen R.T. Ryanodine receptor 1-related disorders: An historical perspective and proposal for a unified nomenclature Skelet. Muscle 2020 10 32 10.1186/s13395-020-00243-4 33190635 PMC7667763 · DOI
  113. [114]Davis M.R. Haan E. Jungbluth H. Sewry C. North K. Muntoni F. Kuntzer T. Lamont P. Bankier A. Tomlinson P. Principal mutation hotspot for central core disease and related myopathies in the C-terminal transmembrane region of the RYR1 gene Neuromuscul. Disord. 2003 13 151 157 10.1016/S0960-8966(02)00218-3 12565913 · DOI
  114. [115]Levano S. Vukcevic M. Singer M. Matter A. Treves S. Urwyler A. Girard T. Increasing the number of diagnostic mutations in malignant hyperthermia Hum. Mutat. 2009 30 590 598 10.1002/humu.20878 19191329 · DOI
  115. [116]Robinson R. Carpenter D. Shaw M.A. Halsall J. Hopkins P. Mutations in RYR1 in malignant hyperthermia and central core disease Hum. Mutat. 2006 27 977 989 10.1002/humu.20356 16917943 · DOI
  116. [117]Wu S. Ibarra M.C. Malicdan M.C. Murayama K. Ichihara Y. Kikuchi H. Nonaka I. Noguchi S. Hayashi Y.K. Nishino I. Central core disease is due to RYR1 mutations in more than 90% of patients Brain 2006 129 1470 1480 10.1093/brain/awl077 16621918 · DOI
  117. [118]Zhou H. Jungbluth H. Sewry C.A. Feng L. Bertini E. Bushby K. Straub V. Roper H. Rose M.R. Brockington M. Molecular mechanisms and phenotypic variation in RYR1-related congenital myopathies Brain 2007 130 2024 2036 10.1093/brain/awm096 17483490 · DOI
  118. [119]Maggi L. Scoto M. Cirak S. Robb S.A. Klein A. Lillis S. Cullup T. Feng L. Manzur A.Y. Sewry C.A. Congenital myopathies—clinical features and frequency of individual subtypes diagnosed over a 5-year period in the United Kingdom Neuromuscul. Disord. 2013 23 195 205 10.1016/j.nmd.2013.01.004 23394784 · DOI
  119. [120]Colombo I. Scoto M. Manzur A.Y. Robb S.A. Maggi L. Gowda V. Cullup T. Yau M. Phadke R. Sewry C. Congenital myopathies: Natural history of a large pediatric cohort Neurology 2015 84 28 35 10.1212/WNL.0000000000001110 25428687 PMC4336094 · DOI
  120. [121]Jungbluth H. Central core disease Orphanet J. Rare Dis. 2007 2 25 10.1186/1750-1172-2-25 17504518 PMC1887524 · DOI
  121. [122]Jungbluth H. Multi-minicore disease Orphanet J. Rare Dis. 2007 2 31 10.1186/1750-1172-2-31 17631035 PMC1947955 · DOI
  122. [123]Clarke N.F. Waddell L.B. Cooper S.T. Perry M. Smith R.L. Kornberg A.J. Muntoni F. Lillis S. Straub V. Bushby K. Recessive mutations in RYR1 are a common cause of congenital fibre type disproportion Hum. Mutat. 2010 31 e1544 e1550 10.1002/humu.21278 20583297 · DOI
  123. [124]Monnier N. Marty I. Faure J. Castiglioni C. Desnuelle C. Sacconi S. Estournet B. Ferreiro A. Romero N. Laquerriere A. Null mutations causing depletion of the type 1 ryanodine receptor (RYR1) are commonly associated with recessive structural congenital myopathies with cores Hum. Mutat. 2008 29 670 678 10.1002/humu.20696 18253926 · DOI
  124. [125]Monnier N. Romero N.B. Lerale J. Nivoche Y. Qi D. MacLennan D.H. Fardeau M. Lunardi J. An autosomal dominant congenital myopathy with cores and rods is associated with a neomutation in the RYR1 gene encoding the skeletal muscle ryanodine receptor Hum. Mol. Genet. 2000 9 2599 2608 10.1093/hmg/9.18.2599 11063719 · DOI
  125. [126]Jungbluth H. Dowling J.J. Ferreiro A. Muntoni F. 182nd ENMC International Workshop: RYR1-related myopathies, 15-17th April 2011, Naarden, The Netherlands Neuromuscul. Disord. 2012 22 453 462 10.1016/j.nmd.2011.12.003 22226685 · DOI
  126. [127]Wilmshurst J.M. Lillis S. Zhou H. Pillay K. Henderson H. Kress W. Müller C.R. Ndondo A. Cloke V. Cullup T. RYR1 mutations are a common cause of congenital myopathies with central nuclei Ann. Neurol. 2010 68 717 726 10.1002/ana.22119 20839240 · DOI
  127. [128]Ferreiro A. Monnier N. Romero N.B. Leroy J.P. Bönnemann C. Haenggeli C.A. Straub V. Voss W.D. Nivoche Y. Jungbluth H. A recessive form of central core disease, transiently presenting as multi-minicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene Ann. Neurol. 2002 51 750 759 10.1002/ana.10231 12112081 · DOI
  128. [129]Romero N.B. Monnier N. Viollet L. Cortey A. Chevallay M. Leroy J.P. Lunardi J. Fardeau M. Dominant and recessive central core disease associated with RYR1 mutations and fetal akinesia Brain 2003 126 2341 2349 10.1093/brain/awg244 12937085 · DOI
  129. [130]De Wel B. Claeys K.G. Malignant hyperthermia: Still an issue for neuromuscular diseases? Curr. Opin. Neurol. 2018 31 628 634 10.1097/WCO.0000000000000592 30015672 · DOI
  130. [131]Carpenter D. Robinson R.L. Quinnell R.J. Ringrose C. Hogg M. Casson F. Booms P. Iles D.E. Halsall P.J. Steele D.S. Genetic variation in RYR1 and malignant hyperthermia phenotypes Br. J. Anaesth. 2009 103 538 548 10.1093/bja/aep204 19648156 · DOI
  131. [132]Rosenberg H. Pollock N. Schiemann A. Bulger T. Stowell K. Malignant hyperthermia: A review Orphanet J. Rare Dis. 2015 10 93 10.1186/s13023-015-0310-1 26238698 PMC4524368 · DOI
  132. [133]Lehmann-Horn F. Iaizzo P.A. Are myotonias and periodic paralyses associated with susceptibility to malignant hyper—thermia? Br. J. Anaesth. 1990 65 692 697 10.1093/bja/65.5.692 2248848 · DOI
  133. [134]Dowling J.J. Lillis S. Amburgey K. Zhou H. Al-Sarraj S. Buk S.J. Wraige E. Chow G. Abbs S. Leber S. King-Denborough syndrome with and without mutations in the skeletal muscle ryanodine receptor (RYR1) gene Neuromuscul. Disord. 2011 21 420 427 10.1016/j.nmd.2011.03.006 21514828 · DOI
  134. [135]Jungbluth H. Lillis S. Zhou H. Abbs S. Sewry C. Swash M. Muntoni F. Late-onset axial myopathy with cores due to a novel heterozygous dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene Neuromuscul. Disord. 2009 19 344 347 10.1016/j.nmd.2009.02.005 19303294 · DOI
  135. [136]Zhou H. Lillis S. Loy R.E. Ghassemi F. Rose M.R. Norwood F. Mills K. Al-Sarraj S. Lane R.J. Feng L. Multi-minicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene Neuromuscul. Disord. 2010 20 166 173 10.1016/j.nmd.2009.12.005 20080402 PMC3136116 · DOI
  136. [137]Bertocchini F. Ovitt C.E. Conti A. Barone V. Schöler H.R. Bottinelli R. Reggiani C. Sorrentino V. Requirement for the ryanodine receptor type 3 for efficient contraction in neonatal skeletal muscles EMBO J. 1997 16 6956 6963 10.1093/emboj/16.23.6956 9384575 PMC1170299 · DOI
  137. [138]Perez C.F. López J.R. Allen P.D. Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle Am. J. Physiol. Cell. Physiol. 2005 88 C640 C649 10.1152/ajpcell.00407.2004 15548569 · DOI
  138. [139]Nilipour Y. Nafissi S. Tjust A.E. Ravenscroft G. Hossein Nejad Nedai H. Taylor R.L. Varasteh V. Pedrosa Domellöf F. Zangi M. Tonekaboni S.H. Ryanodine receptor type 3 (RYR3) as a novel gene associated with a myopathy with nemaline bodies Eur. J. Neurol. 2018 25 841 847 10.1111/ene.13607 29498452 · DOI
  139. [140]Krüger J. Kunert-Keil C. Bisping F. Brinkmeier H. Transient receptor potential cation channels in normal and dystrophic mdx muscle Neuromuscul. Disord. 2008 18 501 513 10.1016/j.nmd.2008.04.003 18504127 · DOI
  140. [141]Ho T.C. Horn N.A. Huynh T. Kelava L. Lansman J.B. Evidence TRPV4 contributes to mechanosensitive ion channels in mouse skeletal muscle fibers Channels 2012 6 246 254 10.4161/chan.20719 22785252 PMC3508903 · DOI
  141. [142]Pritschow B.W. Lange T. Kasch J. Kunert-Keil C. Liedtke W. Brinkmeier H. Functional TRPV4 channels are expressed in mouse skeletal muscle and can modulate resting Ca2+ influx and muscle fatigue Pflug. Arch. 2011 46 115 122 10.1007/s00424-010-0883-4 20924600 · DOI
  142. [143]Auer-Grumbach M. Olschewski A. Papić L. Kremer H. McEntagart M.E. Uhrig S. Fischer C. Fröhlich E. Bálint Z. Tang B. Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C Nat. Genet. 2010 42 160 164 10.1038/ng.508 20037588 PMC3272392 · DOI
  143. [144]Deng H.X. Klein C.J. Yan J. Shi Y. Wu Y. Fecto F. Yau H.J. Yang Y. Zhai H. Siddique N. Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4 Nat. Genet. 2010 42 165 169 10.1038/ng.509 20037587 PMC3786192 · DOI
  144. [145]Landouré G. Zdebik A.A. Martinez T.L. Burnett B.G. Stanescu H.C. Inada H. Shi Y. Taye A.A. Kong L. Munns C.H. Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C Nat. Genet. 2010 42 170 174 10.1038/ng.512 20037586 PMC2812627 · DOI
  145. [146]Zimoń M. Baets J. Auer-Grumbach M. Berciano J. Garcia A. Lopez-Laso E. Merlini L. Hilton-Jones D. McEntagart M. Crosby A.H. Dominant mutations in the cation channel gene transient receptor potential vanilloid 4 cause an unusual spectrum of neuropathies Brain 2010 133 1798 1809 10.1093/brain/awq109 20460441 PMC2912694 · DOI
  146. [147]Rock M.J. Prenen J. Funari V.A. Funari T.L. Merriman B. Nelson S.F. Lachman R.S. Wilcox W.R. Reyno S. Quadrelli R. Gain-of-function mutations in TRPV4 cause autosomal dominant brachyolmia Nat. Genet. 2008 40 999 1003 10.1038/ng.166 18587396 PMC3525077 · DOI
  147. [148]Krakow D. Vriens J. Camacho N. Luong P. Deixler H. Funari T.L. Bacino C.A. Irons M.B. Holm I.A. Sadler L. Mutations in the gene encoding the calcium-permeable ion channel TRPV4 produce spondylometaphyseal dysplasia, Kozlowski type and metatropic dysplasia Am. J. Hum. Genet. 2009 84 307 315 10.1016/j.ajhg.2009.01.021 19232556 PMC2667978 · DOI
  148. [149]Cho T.J. Matsumoto K. Fano V. Dai J. Kim O.H. Chae J.H. Yoo W.J. Tanaka Y. Matsui Y. Takigami I. TRPV4-pathy manifesting both skeletal dysplasia and peripheral neuropathy: A report of three patients Am. J. Med. Genet. A 2012 158A 795 802 10.1002/ajmg.a.35268 22419508 · DOI
  149. [150]Echaniz-Laguna A. Dubourg O. Carlier P. Carlier R.Y. Sabouraud P. Péréon Y. Chapon F. Thauvin-Robinet C. Laforêt P. Eymard B. Phenotypic spectrum and incidence of TRPV4 mutations in patients with inherited axonal neuropathy Neurology 2014 82 1919 1926 10.1212/WNL.0000000000000450 24789864 · DOI
  150. [151]Oonk A.M. Ekker M.S. Huygen P.L. Kunst H.P. Kremer H. Schelhaas J.J. Pennings R.J. Intrafamilial variable hearing loss in TRPV4 induced spinal muscular atrophy Ann. Otol. Rhinol. Laryngol. 2014 123 859 865 10.1177/0003489414539130 24963089 · DOI
  151. [152]Evangelista T. Bansagi B. Pyle A. Griffin H. Douroudis K. Polvikoski T. Antoniadi T. Bushby K. Straub V. Chinnery P.F. Phenotypic variability of TRPV4 related neuropathies Neuromuscul. Disord. 2015 25 516 521 10.1016/j.nmd.2015.03.007 25900305 PMC4454778 · DOI
  152. [153]Koutsis G. Lynch D. Manole A. Karadima G. Reilly M.M. Houlden H. Panas M. Charcot-Marie-Tooth disease type 2C and scapuloperoneal muscular atrophy overlap syndrome in a patient with the R232C TRPV4 mutation J. Neurol. 2015 262 1972 1975 10.1007/s00415-015-7800-x 26048687 · DOI
  153. [154]Ürel-Demir G. Şimşek-Kiper P.Ö. Öncel İ. Utine G.E. Haliloğlu G. Boduroğlu K. Natural history of TRPV4-Related disorders: From skeletal dysplasia to neuromuscular phenotype Eur. J. Paediatr. Neurol. 2021 32 46 55 10.1016/j.ejpn.2021.03.011 33774370 · DOI
  154. [155]Sullivan J.M. Zimanyi C.M. Aisenberg W. Bears B. Chen D.H. Day J.W. Bird T.D. Siskind C.E. Gaudet R. Sumner C.J. Novel mutations highlight the key role of the ankyrin repeat domain in TRPV4-mediated neuropathy Neurol. Genet. 2015 1 e29 10.1212/NXG.0000000000000029 27066566 PMC4811381 · DOI
  155. [156]Woolums B.M. McCray B.A. Sung H. Tabuchi M. Sullivan J.M. Ruppell K.T. Yang Y. Mamah C. Aisenberg W.H. Saavedra-Rivera P.C. TRPV4 disrupts mitochondrial transport and causes axonal degeneration via a CaMKII-dependent elevation of intracellular Ca2+ Nat. Commun. 2020 11 2679 10.1038/s41467-020-16411-5 32471994 PMC7260201 · DOI
  156. [157]Dupont C. Novak K. Denman K. Myers J.H. Sullivan J.M. Walker P.V. 2nd TRPV4 Antagonism Prevents Mechanically Induced Myotonia Ann. Neurol. 2020 88 297 308 10.1002/ana.25780 32418267 PMC7657963 · DOI
  157. [158]Goyal N. Skrdla P. Schroyer R. Kumar S. Fernando D. Oughton A. Norton N. Sprecher D.L. Cheriyan J. Clinical Pharmacokinetics, Safety, and Tolerability of a Novel, First-in-Class TRPV4 Ion Channel Inhibitor, GSK2798745, in Healthy and Heart Failure Subjects Am. J. Cardiovasc. Drugs 2019 19 335 342 10.1007/s40256-018-00320-6 30637626 · DOI
  158. [159]Carter M.T. McMillan H.J. Tomin A. Weiss N. Compound heterozygous CACNA1H mutations associated with severe congenital amyotrophy Channels 2019 13 153 161 10.1080/19336950.2019.1614415 31070086 PMC6527065 · DOI
  159. [160]Tawil R. Ptacek L.J. Pavlakis S.G. DeVivo D.C. Penn A.S. Ozdemir C. Griggs R.C. Andersen’s syndrome: Potassium-sensitive periodic paralysis, ventricular ectopy, and dysmorphic features Ann. Neurol. 1994 35 326 330 10.1002/ana.410350313 8080508 · DOI
  160. [161]Sansone V. Tawil R. Management and treatment of Andersen-Tawil syndrome (ATS) Neurotherapeutics 2007 4 233 237 10.1016/j.nurt.2007.01.005 17395133 · DOI
  161. [162]Pérez-Riera A.R. Barbosa-Barros R. Samesina N. Pastore C.A. Scanavacca M. Daminello-Raimundo R. de Abreu L.C. Nikus K. Brugada P. Andersen-Tawil Syndrome: A Comprehensive Review Cardiol. Rev. 2021 29 165 177 10.1097/CRD.0000000000000326 32947483 · DOI
  162. [163]Nguyen H.L. Pieper G.H. Wilders R. Andersen-Tawil syndrome: Clinical and molecular aspects Int. J. Cardiol. 2013 170 1 16 10.1016/j.ijcard.2013.10.010 24383070 · DOI
  163. [164]Child N.D. Cleland J.C. Roxburgh R. Andersen-Tawil syndrome presenting as a fixed myopathy Muscle Nerve 2013 48 623 10.1002/mus.23872 23568766 · DOI
  164. [165]Lefter S. Hardiman O. Costigan D. Lynch B. McConville J. Hand C.K. Ryan A.M. Andersen-Tawil syndrome with early fixed myopathy J. Clin. Neuromuscul. Dis. 2014 16 79 82 10.1097/CND.0000000000000052 25415519 · DOI
  165. [166]Oz Tuncer G. Teber S. Kutluk M.G. Albayrak P. Deda G. Andersen-Tawil Syndrome with Early Onset Myopathy: 2 Cases J. Neuromuscul. Dis. 2017 4 93 95 10.3233/JND-160188 28106564 · DOI
  166. [167]Wu L. Fang Y. Zhang B.R. Andersen-Tawil syndrome associated with myopathy World J. Emerg. Med. 2020 11 267 269 10.5847/wjem.j.1920-8642.2020.04.012 33014226 PMC7517401 · DOI
  167. [168]Hiraide T. Fukumura S. Yamamoto A. Nakashima M. Saitsu H. Familial periodic paralysis associated with a rare KCNJ5 variant that supposed to have incomplete penetrance Brain. Dev. 2021 43 470 474 10.1016/j.braindev.2020.10.010 33199157 · DOI
  168. [169]Plaster N.M. Tawil R. Tristani-Firouzi M. Canún S. Bendahhou S. Tsunoda A. Donaldson M.R. Iannaccone S.T. Brunt E. Barohn R. Mutations in Kir2.1 cause the developmental and episodic electrical phenotypes of Andersen’s syndrome Cell 2001 105 511 519 10.1016/S0092-8674(01)00342-7 11371347 · DOI
  169. [170]Lopes C.M. Zhang H. Rohacs T. Jin T. Yang J. Logothetis D.E. Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies Neuron 2002 34 933 944 10.1016/S0896-6273(02)00725-0 12086641 · DOI
  170. [171]Ballester L.Y. Benson D.W. Wong B. Law I.H. Mathews K.D. Vanoye C.G. George A.L. Jr. Trafficking-competent and trafficking-defective KCNJ2 mutations in Andersen syndrome Hum. Mutat. 2006 27 388 10.1002/humu.9418 16541386 · DOI
  171. [172]Ma D. Tang X.D. Rogers T.B. Welling P.A. An andersen-Tawil syndrome mutation in Kir2.1 (V302M) alters the G-loop cytoplasmic K+ conduction pathway J. Biol. Chem. 2007 282 5781 5789 10.1074/jbc.M608776200 17166852 · DOI
  172. [173]Handklo-Jamal R. Meisel E. Yakubovich D. Vysochek L. Beinart R. Glikson M. McMullen J.R. Dascal N. Nof E. Oz S. Andersen-Tawil Syndrome Is Associated With Impaired PIP2 Regulation of the Potassium Channel Kir2.1 Front. Pharmacol. 2020 11 672 10.3389/fphar.2020.00672 32499698 PMC7243181 · DOI
  173. [174]Bendahhou S. Donaldson M.R. Plaster N.M. Tristani-Firouzi M. Fu Y.H. Ptácek L.J. Defective potassium channel Kir2.1 trafficking underlies Andersen-Tawil syndrome J. Biol. Chem. 2003 278 51779 51785 10.1074/jbc.M310278200 14522976 · DOI
  174. [175]Bendahhou S. Fournier E. Sternberg D. Bassez G. Furby A. Sereni C. Donaldson M.R. Larroque M.M. Fontaine B. Barhanin J. In vivo and in vitro functional characterization of Andersen’s syndrome mutations J. Physiol. 2005 565 731 741 10.1113/jphysiol.2004.081620 15831539 PMC1464553 · DOI
  175. [176]Sacco S. Giuliano S. Sacconi S. Desnuelle C. Barhanin J. Amri E.Z. Bendahhou S. The inward rectifier potassium channel Kir2.1 is required for osteoblastogenesis Hum. Mol. Genet. 2015 24 471 479 10.1093/hmg/ddu462 25205110 · DOI
  176. [177]Belus M.T. Rogers M.A. Elzubeir A. Josey M. Rose S. Andreeva V. Yelick P.C. Bates E.A. Kir2.1 is important for efficient BMP signaling in mammalian face development Dev. Biol. 2018 444 S297 S307 10.1016/j.ydbio.2018.02.012 29571612 PMC6148416 · DOI
  177. [178]Pini J. Giuliano S. Matonti J. Gannoun L. Simkin D. Rouleau M. Bendahhou S. Osteogenic and Chondrogenic Master Genes Expression Is Dependent on the Kir2.1 Potassium Channel Through the Bone Morphogenetic Protein Pathway J. Bone Miner. Res. 2018 33 1826 1841 10.1002/jbmr.3474 29813186 · DOI
  178. [179]Preisig-Müller R. Schlichthörl G. Goerge T. Heinen S. Brüggemann A. Rajan S. Derst C. Veh R.W. Daut J. Heteromerization of Kir2.x potassium channels contributes to the phenotype of Andersen’s syndrome Proc. Natl. Acad. Sci. USA 2002 99 7774 7779 10.1073/pnas.102609499 12032359 PMC124349 · DOI
  179. [180]Decher N. Renigunta V. Zuzarte M. Soom M. Heinemann S.H. Timothy K.W. Keating M.T. Daut J. Sanguinetti M.C. Splawski I. Impaired interaction between the slide helix and the C-terminus of Kir2.1: A novel mechanism of Andersen syndrome Cardiovasc. Res. 2007 75 748 757 10.1016/j.cardiores.2007.05.010 17568571 · DOI
  180. [181]Jagodzińska M. Szperl M. Ponińska J. Kosiec A. Gajda R. Kukla P. Biernacka E.K. Coexistence of Andersen-Tawil Syndrome with Polymorphisms in hERG1 Gene (K897T) and SCN5A Gene (H558R) in One Family Ann. Noninvasive Electrocardiol. 2016 21 189 195 10.1111/anec.12283 26109178 PMC6931717 · DOI
  181. [182]Polyak M.E. Shestak A. Podolyak D. Zaklyazminskaya E. Compound heterozygous mutations in KCNJ2 and KCNH2 in a patient with severe Andersen-Tawil syndrome BMJ Case Rep. 2020 13 e235703 10.1136/bcr-2020-235703 PMC7449271 32843460 · DOI
  182. [183]Priori S.G. Pandit S.V. Rivolta I. Berenfeld O. Ronchetti E. Dhamoon A. Napolitano C. Anumonwo J. Di Barletta M.R. Gudapakkam S. A novel form of short QT syndrome (SQT3) is caused by a mutation in the KCNJ2 gene Circ. Res. 2005 96 800 807 10.1161/01.RES.0000162101.76263.8c 15761194 · DOI
  183. [184]Xia M. Jin Q. Bendahhou S. He Y. Larroque M.M. Chen Y. Zhou Q. Yang Y. Liu Y. Liu B. A Kir2.1 gain-of-function mutation underlies familial atrial fibrillation Biochem. Biophys. Res. Commun. 2005 332 1012 1019 10.1016/j.bbrc.2005.05.054 15922306 · DOI
  184. [185]Yang Y. Yang Y. Liang B. Liu J. Li J. Grunnet M. Olesen S.P. Rasmussen H.B. Ellinor P.T. Gao L. Identification of a Kir3.4 mutation in congenital long QT syndrome Am. J. Hum. Genet. 2010 86 872 880 10.1016/j.ajhg.2010.04.017 20560207 PMC3032079 · DOI
  185. [186]Kokunai Y. Nakata T. Furuta M. Sakata S. Kimura H. Aiba T. Yoshinaga M. Osaki Y. Nakamori M. Itoh H. A Kir3.4 mutation causes Andersen-Tawil syndrome by an inhibitory effect on Kir2.1 Neurology 2014 82 1058 1064 10.1212/WNL.0000000000000239 24574546 · DOI
  186. [187]Nagamine S. Sakoda S. Koide R. Kawata A. Yuan J. Takashima H. Nakano I. A case of Andersen-Tawil syndrome presenting periodic paralysis exacerbated by ACZ J. Neurol. Sci. 2014 347 385 386 10.1016/j.jns.2014.09.040 25284084 · DOI
  187. [190]Sternberg D. Tabti N. Fournier E. Hainque B. Fontaine B. Lack of association of the potassium channel-associated peptide MiRP2-R83H variant with periodic paralysis Neurology 2003 61 857 859 10.1212/01.WNL.0000082392.66713.E3 14504341 · DOI
  188. [191]Jurkat-Rott K. Lehmann-Horn F. Periodic paralysis mutation MiRP2-R83H in controls: Interpretations and general recommendation Neurology 2004 62 1012 1015 10.1212/01.WNL.0000119392.29624.88 15037716 · DOI
  189. [192]Tang N.L. Chow C.C. Ko G.T. Tai M.H. Kwok R. Yao X.Q. Cockram C.S. No mutation in the KCNE3 potassium channel gene in Chinese thyrotoxic hypokalaemic periodic paralysis patients Clin. Endocrinol. 2004 61 109 112 10.1111/j.1365-2265.2004.02079.x 15212652 · DOI
  190. [193]Abbott G.W. Butler M.H. Goldstein S.A. Phosphorylation and protonation of neighboring MiRP2 sites: Function and pathophysiology of MiRP2-Kv3.4 potassium channels in periodic paralysis FASEB J. 2006 20 293 301 10.1096/fj.05-5070com 16449802 · DOI
  191. [194]Portaro S. Altamura C. Licata N. Camerino G.M. Imbrici P. Musumeci O. Rodolico C. Camerino D.C. Toscano A. Desaphy J.F. Clinical, Molecular, and Functional Characterization of CLCN1 Mutations in Three Families with Recessive Myotonia Congenita Neuromol. Med. 2015 17 285 296 10.1007/s12017-015-8356-8 26007199 PMC4534513 · DOI
  192. [195]Imbrici P. Accogli A. Blunck R. Altamura C. Iacomino M. D’adamo M.C. Allegri A. Pedemonte M. Brolatti N. Vari S. Musculoskeletal Features without Ataxia Associated with a Novel de novo Mutation in KCNA1 Impairing the Voltage Sensitivity of Kv1.1 Channel Biomedicines 2021 9 75 10.3390/biomedicines9010075 33466780 PMC7829709 · DOI
  193. [196]Salih M. van Kinschot C.M. Peeters R.P. de Herder W.W. Duschek E.J. Van Der Linden J. van Noord C. Thyrotoxic periodic paralysis: An unusual presentation of hyperthyroidism Neth. J. Med. 2017 75 315 320 29219824
  194. [197]Chu P.Y. Cheng C.J. Tseng M.H. Yang S.S. Chen H.C. Lin S.H. Genetic variant rs623011 (17q24.3) associates with non-familial thyrotoxic and sporadic hypokalemic paralysis Clin. Chim. Acta 2012 414 105 108 10.1016/j.cca.2012.08.004 22910584 · DOI · Paper page
  195. [198]Song I.W. Sung C.C. Chen C.H. Cheng C.J. Yang S.S. Chou Y.C. Yang J.H. Chen Y.T. Wu J.Y. Lin S.H. Novel susceptibility gene for nonfamilial hypokalemic periodic paralysis Neurology 2016 86 1190 1198 10.1212/WNL.0000000000002524 26935888 · DOI
  196. [199]Nakaza M. Kitamura Y. Furuta M. Kubota T. Sasaki R. Takahashi M.P. Analysis of the genetic background associated with sporadic periodic paralysis in Japanese patients J. Neurol. Sci. 2020 412 116795 10.1016/j.jns.2020.116795 32234253 · DOI
  197. [200]Cannon S.C. Further evidence for shared genetic susceptibility in both sporadic and thyrotoxic periodic paralysis J. Neurol. Sci. 2020 412 116794 10.1016/j.jns.2020.116794 32229026 PMC8137387 · DOI
  198. [201]Ryan D.P. Da Silva M.R. Soong T.W. Fontaine B. Donaldson M.R. Kung A.W. Jongjaroenprasert W. Liang M.C. Khoo D.H. Cheah J.S. Mutations in potassium channel Kir2.6 cause susceptibility to thyrotoxic hypokalemic periodic paralysis Cell 2010 140 88 98 10.1016/j.cell.2009.12.024 20074522 PMC2885139 · DOI · Paper page
  199. [203]Zheng J. Liang Z. Hou Y. Liu F. Hu Y. Lin P. Yan C. A novel Kir2.6 mutation associated with hypokalemic periodic paralysis Clin. Neurophysiol. 2016 127 2503 2508 10.1016/j.clinph.2016.03.008 27178871 · DOI
  200. [204]Paninka R.M. Carlos-Lima E. Lindsey S.C. Kunii I.S. Dias-da-Silva M.R. Arcisio-Miranda M. Down-regulation of Kir2.6 channel by c-termini mutation D252N and its association with the susceptibility to Thyrotoxic Periodic Paralysis Neuroscience 2017 346 197 202 10.1016/j.neuroscience.2017.01.019 28131627 · DOI

200 of 265 shown

Cited by

Sorted by citations

Authors
Maggi, L., Bonanno, S., Altamura, C., & Desaphy, J.-F.
Affiliations
  • Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
  • University of Bari Aldo Moro (IT)
Corresponding author
Maggi, Lorenzo
ORCID
Venue
Cells
Publisher
MDPI AG
Published
2021-06-16
Volume
10
Issue
6
Pages
1521
ISSN
2073-4409 (ISSN-L)
DOI
10.3390/cells10061521
PMC
PMC8234207
OpenAlex
W3166411417
Cited by
51
References
5
Citations by year
2026: 6 · 2025: 14 · 2024: 9 · 2023: 10 · 2022: 10 · 2021: 2
FWCI
0.81
Type
journal article
Language
en
Open access
Licence
Locations
  • Cells (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion, cc-by)
Funders
  • Association Française contre les Myopathies (16123)
  • Universita degli Studi di Bari Aldo Moro (2017–2018)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
Keywords
ion channel mutations, myotonia, periodic paralysis, progressive myopathy, pathogenesis
MeSH terms
Animals, Humans, Ion Channels, Muscular Diseases, Mutation, Muscle, Skeletal, Channelopathies

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review