{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T02:08:58Z","timestamp":1777601338228,"version":"3.51.4"},"reference-count":112,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2023,1,1]],"date-time":"2023-01-01T00:00:00Z","timestamp":1672531200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,1,1]],"date-time":"2023-01-01T00:00:00Z","timestamp":1672531200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,12,6]],"date-time":"2022-12-06T00:00:00Z","timestamp":1670284800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/V002767\/1"],"award-info":[{"award-number":["BB\/V002767\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["PG\/21\/10521"],"award-info":[{"award-number":["PG\/21\/10521"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["FS\/17\/56\/32925"],"award-info":[{"award-number":["FS\/17\/56\/32925"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["JCS-180802"],"award-info":[{"award-number":["JCS-180802"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["102172\/B\/13\/Z"],"award-info":[{"award-number":["102172\/B\/13\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000836","name":"University of Liverpool","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000836","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2023,1]]},"DOI":"10.1016\/j.jbc.2022.102777","type":"journal-article","created":{"date-parts":[[2022,12,8]],"date-time":"2022-12-08T02:18:38Z","timestamp":1670465918000},"page":"102777","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"title":["Calmodulin variant E140G associated with long QT syndrome impairs CaMKII\u03b4 autophosphorylation and L-type calcium channel inactivation"],"prefix":"10.1016","volume":"299","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9379-7490","authenticated-orcid":false,"given":"Ohm","family":"Prakash","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nitika","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amy","family":"Milburn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Liam","family":"McCormick","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vishvangi","family":"Deugi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pauline","family":"Fisch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jacob","family":"Wyles","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N Lowri","family":"Thomas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Svetlana","family":"Antonyuk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Caroline","family":"Dart","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nordine","family":"Helassa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.102777_bib1","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1161\/CIRCULATIONAHA.109.863209","article-title":"Prevalence of the congenital long-QT syndrome","volume":"120","author":"Schwartz","year":"2009","journal-title":"Circulation"},{"key":"10.1016\/j.jbc.2022.102777_bib2","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1161\/CIRCGENETICS.116.001571","article-title":"New insights into the genetic basis of inherited arrhythmia syndromes","volume":"9","author":"Gray","year":"2016","journal-title":"Circ. Cardiovasc. Genet."},{"key":"10.1016\/j.jbc.2022.102777_bib3","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1016\/j.jacc.2018.01.078","article-title":"Interplay between genetic substrate, QTc duration, and arrhythmia risk in patients with long QT syndrome","volume":"71","author":"Mazzanti","year":"2018","journal-title":"J.\u00a0Am. Coll. Cardiol."},{"key":"10.1016\/j.jbc.2022.102777_bib4","doi-asserted-by":"crossref","first-page":"556","DOI":"10.3390\/life12040556","article-title":"KCNH2 p.Gly262AlafsTer98: a new threatening variant associated with long QT syndrome in a Spanish cohort","volume":"12","author":"Lorca","year":"2022","journal-title":"Life"},{"key":"10.1016\/j.jbc.2022.102777_bib5","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/s41572-020-0188-7","article-title":"Inherited cardiac arrhythmias","volume":"6","author":"Schwartz","year":"2020","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.jbc.2022.102777_bib6","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1007\/s00246-012-0303-y","article-title":"Cardiac sodium channel Nav1.5 mutations and cardiac arrhythmia","volume":"33","author":"Song","year":"2012","journal-title":"Pediatr. Cardiol."},{"key":"10.1016\/j.jbc.2022.102777_bib7","doi-asserted-by":"crossref","first-page":"396","DOI":"10.3389\/fnmol.2018.00396","article-title":"Human calmodulin mutations","volume":"11","author":"Jensen","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.jbc.2022.102777_bib8","doi-asserted-by":"crossref","first-page":"2964","DOI":"10.1093\/eurheartj\/ehz311","article-title":"Calmodulin mutations and life-threatening cardiac arrhythmias: insights from the international calmodulinopathy registry","volume":"40","author":"Crotti","year":"2019","journal-title":"Eur. Heart J."},{"key":"10.1016\/j.jbc.2022.102777_bib9","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1161\/CIRCULATIONAHA.112.001216","article-title":"Calmodulin mutations associated with recurrent cardiac arrest in infants","volume":"127","author":"Crotti","year":"2013","journal-title":"Circulation"},{"key":"10.1016\/j.jbc.2022.102777_bib10","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.hrcr.2016.02.002","article-title":"Novel CALM3 mutations in pediatric long QT syndrome patients support a CALM3-specific calmodulinopathy","volume":"2","author":"Chaix","year":"2016","journal-title":"Heartrhythm Case Rep."},{"key":"10.1016\/j.jbc.2022.102777_bib11","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1161\/CIRCGENETICS.115.001323","article-title":"Spectrum and prevalence of CALM1-, CALM2-, and CALM3-encoded calmodulin variants in Long QT syndrome and functional characterization of a novel Long QT syndrome-associated calmodulin missense variant, E141G","volume":"9","author":"Boczek","year":"2016","journal-title":"Circ. Cardiovasc. Genet."},{"key":"10.1016\/j.jbc.2022.102777_bib12","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.hrthm.2014.10.035","article-title":"CALM3 mutation associated with long QT syndrome","volume":"12","author":"Reed","year":"2015","journal-title":"Heart Rhythm"},{"key":"10.1016\/j.jbc.2022.102777_bib13","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0153851","article-title":"Calmodulin 2 mutation N98S is associated with unexplained cardiac arrest in infants due to low clinical penetrance electrical disorders","volume":"11","author":"Jimenez-Jaimez","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102777_bib14","doi-asserted-by":"crossref","DOI":"10.1161\/CIRCGEN.119.002581","article-title":"Genetic mosaicism in calmodulinopathy","volume":"12","author":"Wren","year":"2019","journal-title":"Circ. Genomic Precision Med."},{"key":"10.1016\/j.jbc.2022.102777_bib15","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1111\/ped.13959","article-title":"Long QT syndrome with a de novo CALM2 mutation in a 4-year-old boy","volume":"61","author":"Fujita","year":"2019","journal-title":"Pediatr. Int."},{"key":"10.1016\/j.jbc.2022.102777_bib16","doi-asserted-by":"crossref","DOI":"10.1161\/CIRCEP.121.010572","article-title":"Novel CALM3 variant causing calmodulinopathy with variable expressivity in a 4-generation family","volume":"15","author":"Kato","year":"2022","journal-title":"Circ. Arrhythm Electrophysiol."},{"key":"10.1016\/j.jbc.2022.102777_bib17","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1161\/CIRCGENETICS.113.000459","article-title":"Novel calmodulin mutations associated with congenital arrhythmia susceptibility","volume":"7","author":"Makita","year":"2014","journal-title":"Circ. Cardiovasc. Genet."},{"key":"10.1016\/j.jbc.2022.102777_bib18","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.1016\/j.hrthm.2016.06.038","article-title":"Novel calmodulin mutations associated with congenital long QT syndrome affect calcium current in human cardiomyocytes","volume":"13","author":"Pipilas","year":"2016","journal-title":"Heart Rhythm"},{"key":"10.1016\/j.jbc.2022.102777_bib19","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.hrcr.2016.09.004","article-title":"A\u00a0novel de novo calmodulin mutation in a 6-year-old boy who experienced an aborted cardiac arrest","volume":"3","author":"Takahashi","year":"2017","journal-title":"Heartrhythm Case Rep."},{"key":"10.1016\/j.jbc.2022.102777_bib20","doi-asserted-by":"crossref","first-page":"15","DOI":"10.4103\/tcmj.tcmj_285_20","article-title":"Calmodulin: the switch button of calcium signaling","volume":"34","author":"Yang","year":"2022","journal-title":"Tzu Chi Med. J."},{"key":"10.1016\/j.jbc.2022.102777_bib21","doi-asserted-by":"crossref","first-page":"17185","DOI":"10.1073\/pnas.262372999","article-title":"Engineered calmodulins reveal the unexpected eminence of Ca2+ channel inactivation in controlling heart excitation","volume":"99","author":"Alseikhan","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102777_bib22","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/S0896-6273(00)80709-6","article-title":"Calmodulin is the Ca2+ sensor for Ca2+-dependent inactivation of L-type calcium channels","volume":"22","author":"Peterson","year":"1999","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2022.102777_bib23","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1038\/20200","article-title":"Calmodulin supports both inactivation and facilitation of L-type calcium channels","volume":"399","author":"Zuhlke","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102777_bib24","doi-asserted-by":"crossref","first-page":"691341","DOI":"10.5402\/2012\/691341","article-title":"Molecular determinants of Cav1.2 calcium channel inactivation","volume":"2012","author":"Soldatov","year":"2012","journal-title":"ISRN Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib25","doi-asserted-by":"crossref","first-page":"20144","DOI":"10.1074\/jbc.M010771200","article-title":"Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)","volume":"276","author":"Balshaw","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00232-001-0111-4","article-title":"Modulation of intracellular calcium-release channels by calmodulin","volume":"185","author":"Balshaw","year":"2002","journal-title":"J.\u00a0Membr. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib27","doi-asserted-by":"crossref","first-page":"23480","DOI":"10.1074\/jbc.M301125200","article-title":"Molecular basis of calmodulin binding to cardiac muscle Ca2+ release channel (ryanodine receptor)","volume":"278","author":"Yamaguchi","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib28","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0005-2736(84)90083-X","article-title":"Calmodulin\u00b7(Ca2+)4 is the active calmodulin-calcium species activating the calcium-, calmodulin-dependent protein kinase of cardiac sarcoplasmic reticulum in the regulation of the calcium pump","volume":"773","author":"Pifl","year":"1984","journal-title":"Biochim. Biophys. Acta (Bba) - Biomembr."},{"key":"10.1016\/j.jbc.2022.102777_bib29","doi-asserted-by":"crossref","first-page":"45004","DOI":"10.1074\/jbc.M407286200","article-title":"Calmodulin mediates Ca2+ sensitivity of sodium channels","volume":"279","author":"Kim","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib30","doi-asserted-by":"crossref","first-page":"3558","DOI":"10.1073\/pnas.1114748109","article-title":"Crystallographic basis for calcium regulation of sodium channels","volume":"109","author":"Sarhan","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102777_bib31","doi-asserted-by":"crossref","first-page":"8846","DOI":"10.1074\/jbc.M806871200","article-title":"Functional interactions between distinct sodium channel cytoplasmic domains through the action of calmodulin","volume":"284","author":"Potet","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib32","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1161\/01.RES.0000218863.44140.f2","article-title":"KCNQ1 assembly and function is blocked by long-QT syndrome mutations that disrupt interaction with calmodulin","volume":"98","author":"Ghosh","year":"2006","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib33","doi-asserted-by":"crossref","first-page":"4141","DOI":"10.1074\/jbc.M110.158865","article-title":"KCNE4 juxtamembrane region is required for interaction with calmodulin and for functional suppression of KCNQ1","volume":"286","author":"Ciampa","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib34","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1042\/BCJ20180545","article-title":"Ca2+-dependent calmodulin binding to cardiac ryanodine receptor (RyR2) calmodulin-binding domains","volume":"476","author":"Brohus","year":"2019","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2022.102777_bib35","doi-asserted-by":"crossref","first-page":"1907","DOI":"10.1016\/j.bpj.2009.07.027","article-title":"Ca2+-Calmodulin increases RyR2 open probability yet reduces ryanoid association with RyR2","volume":"97","author":"Sigalas","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102777_bib36","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/1440-1681.12669","article-title":"The emerging role of calmodulin regulation of RyR2 in controlling heart rhythm, the progression of heart failure and the antiarrhythmic action of dantrolene","volume":"44","author":"Walweel","year":"2017","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"10.1016\/j.jbc.2022.102777_bib37","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1016\/S0006-3495(04)74155-7","article-title":"Mechanism of calmodulin inhibition of cardiac sarcoplasmic reticulum Ca2+ release channel (ryanodine receptor)","volume":"86","author":"Xu","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102777_bib38","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1172\/JCI29515","article-title":"Early cardiac hypertrophy in mice with impaired calmodulin regulation of cardiac muscle Ca2+ release channel","volume":"117","author":"Yamaguchi","year":"2007","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2022.102777_bib39","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1161\/CIRCRESAHA.114.302857","article-title":"Cardiac myocyte Z-line calmodulin is mainly RyR2-bound, and reduction is arrhythmogenic and occurs in heart failure","volume":"114","author":"Yang","year":"2014","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib40","doi-asserted-by":"crossref","first-page":"9798","DOI":"10.3390\/ijms22189798","article-title":"Calmodulin interactions with voltage-gated sodium channels","volume":"22","author":"Wu","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib41","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1080\/19336950.2015.1075677","article-title":"Calmodulin and Ca2+ control of voltage gated Na+ channels","volume":"10","author":"Gabelli","year":"2016","journal-title":"Channels"},{"key":"10.1016\/j.jbc.2022.102777_bib42","article-title":"Elementary mechanisms of calmodulin regulation of NaV1.5 producing divergent arrhythmogenic phenotypes","volume":"118","author":"Kang Po","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102777_bib43","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1073\/pnas.0507397103","article-title":"Calcium-dependent regulation of the voltage-gated sodium channel hH1: intrinsic and extrinsic sensors use a common molecular switch","volume":"103","author":"Shah Vikas","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102777_bib44","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1161\/01.RES.0000218979.40770.69","article-title":"Calmodulin is essential for cardiac IKS channel gating and assembly","volume":"98","author":"Shamgar","year":"2006","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib45","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abd6798","article-title":"Calmodulin acts as a state-dependent switch to control a cardiac potassium channel opening","volume":"6","author":"Kang","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2022.102777_bib46","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.yjmcc.2019.03.018","article-title":"Calmodulin inhibition of human RyR2 channels requires phosphorylation of RyR2-S2808 or RyR2-S2814","volume":"130","author":"Walweel","year":"2019","journal-title":"J.\u00a0Mol. Cell Cardiol."},{"key":"10.1016\/j.jbc.2022.102777_bib47","doi-asserted-by":"crossref","first-page":"17907","DOI":"10.1016\/S0021-9258(19)84658-6","article-title":"Tissue-specific expression of four types of rat calmodulin-dependent protein kinase II mRNAs","volume":"264","author":"Tobimatsu","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib48","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.gene.2003.08.023","article-title":"Organization and evolution of multifunctional Ca2+\/CaM-dependent protein kinase genes","volume":"322","author":"Tombes","year":"2003","journal-title":"Gene"},{"key":"10.1016\/j.jbc.2022.102777_bib49","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1016\/j.cardiores.2006.12.009","article-title":"Multiple downstream proarrhythmic targets for calmodulin kinase II: moving beyond an ion channel-centric focus","volume":"73","author":"Anderson","year":"2007","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib50","series-title":"Structure and Function of Sarcoplasmic Reticulum","first-page":"521","article-title":"The calcium-induced calcium release from the sarcoplasmic reticulum","author":"Endo","year":"1985"},{"key":"10.1016\/j.jbc.2022.102777_bib51","doi-asserted-by":"crossref","first-page":"e63","DOI":"10.1161\/CIRCRESAHA.120.318429","article-title":"Ca2+-CaM dependent inactivation of RyR2 underlies Ca2+ alternans in intact heart","volume":"128","author":"Wei","year":"2021","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib52","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/j.bbagen.2011.12.012","article-title":"Ca2+-dependent modulation of voltage-gated Ca2+ channels","volume":"1820","author":"Christel","year":"2012","journal-title":"Biochim. Biophys. Acta (Bba) - Gen. Subj."},{"key":"10.1016\/j.jbc.2022.102777_bib53","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1161\/01.RES.75.5.854","article-title":"Multifunctional Ca2+\/calmodulin-dependent protein kinase mediates Ca2+-induced enhancement of the L-type Ca2+ current in rabbit ventricular myocytes","volume":"75","author":"Anderson","year":"1994","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib54","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1000426","article-title":"Structure of the CaMKIIdelta\/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation","volume":"8","author":"Rellos","year":"2010","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib55","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1126\/science.256.5060.1199","article-title":"Calmodulin trapping by calcium-calmodulin-dependent protein kinase","volume":"256","author":"Meyer","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102777_bib56","doi-asserted-by":"crossref","first-page":"25560","DOI":"10.1074\/jbc.M508661200","article-title":"Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: identification of the phosphorylation sites","volume":"281","author":"Lee","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib57","doi-asserted-by":"crossref","first-page":"167","DOI":"10.2170\/physiolsci.RP000507","article-title":"Distinct roles of CaM and Ca2+\/CaM-dependent protein kinase II in Ca2+-dependent facilitation and inactivation of cardiac L-type Ca2+ channels","volume":"57","author":"Nie","year":"2007","journal-title":"J.\u00a0Physiol. Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib58","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib59","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1038\/nature06529","article-title":"A\u00a0modular switch for spatial Ca2+ selectivity in the calmodulin regulation of CaV channels","volume":"451","author":"Dick","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102777_bib60","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1016\/S0006-3495(03)74586-X","article-title":"Apocalmodulin and Ca2+ calmodulin-binding sites on the CaV1.2 channel","volume":"85","author":"Tang","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102777_bib61","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/B978-0-12-374841-6.00001-3","article-title":"A\u00a0practical guide to the preparation of Ca2+ buffers","volume":"99","author":"Bers","year":"2010","journal-title":"Met. Cell Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib62","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S0092-8674(02)00682-7","article-title":"Calmodulin in action: diversity in target recognition and activation mechanisms","volume":"108","author":"Hoeflich","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2022.102777_bib63","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S0896-6273(04)00081-9","article-title":"Identification of the components controlling inactivation of voltage-gated Ca2+ channels","volume":"41","author":"Kim","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2022.102777_bib64","doi-asserted-by":"crossref","first-page":"a003996","DOI":"10.1101\/cshperspect.a003996","article-title":"Ryanodine receptors: structure, expression, molecular details, and function in calcium release","volume":"2","author":"Lanner","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib65","doi-asserted-by":"crossref","first-page":"30794","DOI":"10.1074\/jbc.M104959200","article-title":"Molecular basis of calmodulin tethering and Ca2+-dependent inactivation of L-type Ca2+ channels","volume":"276","author":"Pitt","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib66","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1161\/01.RES.0000064566.91495.0C","article-title":"Calmodulin regulation of excitation-contraction coupling in cardiac myocytes","volume":"92","author":"Yang","year":"2003","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib67","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1161\/01.RES.0000194329.41863.89","article-title":"Ca2+\/calmodulin-dependent protein kinase modulates cardiac ryanodine receptor phosphorylation and sarcoplasmic reticulum Ca2+ leak in heart failure","volume":"97","author":"Ai","year":"2005","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib68","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.3390\/ijms21041418","article-title":"Calmodulin mutations associated with heart arrhythmia: a status report","volume":"21","author":"Chazin","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib69","doi-asserted-by":"crossref","first-page":"17055","DOI":"10.1016\/S0021-9258(18)37497-0","article-title":"Multiple divergent mRNAs code for a single human calmodulin","volume":"263","author":"Fischer","year":"1988","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib70","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0143-4160(98)90028-8","article-title":"Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3","volume":"23","author":"Toutenhoofd","year":"1998","journal-title":"Cell Calcium"},{"key":"10.1016\/j.jbc.2022.102777_bib71","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1113\/JP279307","article-title":"Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca(2+) binding and cause misfolding","volume":"598","author":"Wang","year":"2020","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.jbc.2022.102777_bib72","doi-asserted-by":"crossref","first-page":"e61","DOI":"10.1161\/01.RES.0000125626.33738.E2","article-title":"Ca2+\/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor","volume":"94","author":"Wehrens","year":"2004","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib73","doi-asserted-by":"crossref","first-page":"38593","DOI":"10.1074\/jbc.M301180200","article-title":"Stoichiometric phosphorylation of cardiac ryanodine receptor on serine 2809 by calmodulin-dependent kinase II and protein kinase A","volume":"278","author":"Rodriguez","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib74","doi-asserted-by":"crossref","first-page":"11144","DOI":"10.1016\/S0021-9258(18)99140-4","article-title":"Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity","volume":"266","author":"Witcher","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib75","doi-asserted-by":"crossref","first-page":"4963","DOI":"10.1016\/S0021-9258(18)42924-9","article-title":"Cardiac-specific phosphorylation site for multifunctional Ca2+\/calmodulin-dependent protein kinase is conserved in the brain ryanodine receptor","volume":"267","author":"Witcher","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib76","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1083\/jcb.200505155","article-title":"CaMKII tethers to L-type Ca2+ channels, establishing a local and dedicated integrator of Ca2+ signals for facilitation","volume":"171","author":"Hudmon","year":"2005","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib77","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1161\/CIRCRESAHA.114.303391","article-title":"Divergent regulation of ryanodine receptor 2 calcium release channels by arrhythmogenic human calmodulin missense mutants","volume":"114","author":"Hwang","year":"2014","journal-title":"Circ. Res."},{"key":"10.1016\/j.jbc.2022.102777_bib78","doi-asserted-by":"crossref","first-page":"26636","DOI":"10.1074\/jbc.M116.758680","article-title":"The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish","volume":"291","author":"Berchtold","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib79","doi-asserted-by":"crossref","first-page":"jcs258796","DOI":"10.1242\/jcs.258796","article-title":"CPVT-associated calmodulin variants N53I and A102V dysregulate Ca2+ signalling via different mechanisms","volume":"135","author":"Prakash","year":"2022","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib80","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.ceca.2006.07.011","article-title":"Free and bound intracellular calmodulin measurements in cardiac myocytes","volume":"41","author":"Wu","year":"2007","journal-title":"Cell Calcium"},{"key":"10.1016\/j.jbc.2022.102777_bib81","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.1016\/S0006-3495(97)78216-X","article-title":"Intracellular Ca2+ inactivates L-type Ca2+ channels with a Hill coefficient of approximately 1 and an inhibition constant of approximately 4 microM by reducing channel's open probability","volume":"73","author":"H\u00f6fer","year":"1997","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2022.102777_bib82","doi-asserted-by":"crossref","first-page":"C991","DOI":"10.1152\/ajpcell.00019.2020","article-title":"The LQT-associated calmodulin mutant E141G induces disturbed Ca2+-dependent binding and a flickering gating mode of the CaV1.2 channel","volume":"318","author":"Su","year":"2020","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.jbc.2022.102777_bib83","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.yjmcc.2014.04.022","article-title":"Calmodulin mutations associated with long QT syndrome prevent inactivation of cardiac L-type Ca2+ currents and promote proarrhythmic behavior in ventricular myocytes","volume":"74","author":"Limpitikul","year":"2014","journal-title":"J.\u00a0Mol. Cell Cardiol."},{"key":"10.1016\/j.jbc.2022.102777_bib84","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1016\/j.str.2005.09.021","article-title":"Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel","volume":"13","author":"Fallon","year":"2005","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102777_bib85","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1254\/jphs.09342FP","article-title":"Interactions of calmodulin with the multiple binding sites of Cav1.2 Ca2+ channels","volume":"112","author":"Asmara","year":"2010","journal-title":"J.\u00a0Pharmacol. Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib86","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0061765","article-title":"The calmodulin-binding, short linear motif, NSCaTE is conserved in L-type channel ancestors of vertebrate Cav1.2 and Cav1.3 channels","volume":"8","author":"Taiakina","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102777_bib87","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1038\/nsmb1027","article-title":"Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain\u2013Ca2+\/calmodulin complex","volume":"12","author":"Van Petegem","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib88","doi-asserted-by":"crossref","first-page":"38","DOI":"10.3389\/fnmol.2012.00038","article-title":"Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca2+-calmodulin","volume":"5","author":"Liu","year":"2012","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.jbc.2022.102777_bib89","doi-asserted-by":"crossref","first-page":"337","DOI":"10.4161\/chan.3.5.9686","article-title":"Characterization of the calmodulin-binding site in the N terminus of CaV1.2","volume":"3","author":"Benmocha","year":"2009","journal-title":"Channels"},{"key":"10.1016\/j.jbc.2022.102777_bib90","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1126\/science.1093490","article-title":"Functional stoichiometry and local enrichment of calmodulin interacting with Ca2+ channels","volume":"304","author":"Mori Masayuki","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102777_bib91","doi-asserted-by":"crossref","first-page":"14948","DOI":"10.1074\/jbc.RA120.013777","article-title":"CaV channels reject signaling from a second CaM in eliciting Ca2+-dependent feedback regulation","volume":"295","author":"Chakouri","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib92","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1126\/science.270.5241.1502","article-title":"Essential Ca2+-binding motif for Ca2+-sensitive inactivation of L-type Ca2+ channels","volume":"270","author":"de Leon","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102777_bib93","doi-asserted-by":"crossref","first-page":"21121","DOI":"10.1074\/jbc.M002986200","article-title":"Ca2+-sensitive inactivation and facilitation of L-type Ca2+ channels both depend on specific amino acid residues in a consensus calmodulin-binding motif in the\u03b11C subunit","volume":"275","author":"Z\u00fchlke","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib94","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1080\/19336950.2020.1750189","article-title":"The CaMKII phosphorylation site Thr1604 in the CaV1.2 channel is involved in pathological myocardial hypertrophy in rats","volume":"14","author":"Li","year":"2020","journal-title":"Channels"},{"key":"10.1016\/j.jbc.2022.102777_bib95","doi-asserted-by":"crossref","first-page":"4554","DOI":"10.1111\/febs.14969","article-title":"Diminished inhibition and facilitated activation of RyR2-mediated Ca(2+) release is a common defect of arrhythmogenic calmodulin mutations","volume":"286","author":"Sondergaard","year":"2019","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2022.102777_bib96","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1007\/s00395-021-00900-9","article-title":"Cardiomyocyte Na(+) and Ca(2+) mishandling drives vicious cycle involving CaMKII, ROS, and ryanodine receptors","volume":"116","author":"Hegyi","year":"2021","journal-title":"Basic Res. Cardiol."},{"key":"10.1016\/j.jbc.2022.102777_bib97","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1007\/s12576-009-0033-y","article-title":"CaMKII phosphorylates a threonine residue in the C-terminal tail of Cav1.2 Ca(2+) channel and modulates the interaction of the channel with calmodulin","volume":"59","author":"Wang","year":"2009","journal-title":"J.\u00a0Physiol. Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib98","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1074\/jbc.M116.766253","article-title":"The arrhythmogenic calmodulin p.Phe142Leu mutation impairs C-domain Ca2+ binding but not calmodulin-dependent inhibition of the cardiac ryanodine receptor","volume":"292","author":"Sondergaard","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102777_bib99","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/0003-9861(87)90048-8","article-title":"Calcium . calmodulin-dependent protein kinase II and calcium . phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide","volume":"252","author":"Hashimoto","year":"1987","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2022.102777_bib100","series-title":"The Proteomics Protocols Handbook","first-page":"571","article-title":"Protein identification and analysis tools on the ExPASy server","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.jbc.2022.102777_bib101","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"Schindelin","year":"2012","journal-title":"Nat. Met."},{"key":"10.1016\/j.jbc.2022.102777_bib102","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1107\/S2059798317017235","article-title":"DIALS: implementation and evaluation of a new integration package","volume":"74","author":"Winter","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib103","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102777_bib104","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1107\/S0907444905036693","article-title":"Scaling and assessment of data quality","volume":"62","author":"Evans","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102777_bib105","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1107\/S2059798317016035","article-title":"CCP4i2: the new graphical user interface to the CCP4 program suite","volume":"74","author":"Potterton","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102777_bib106","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102777_bib107","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jbc.2022.102777_bib108","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102777_bib109","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102777_bib110","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1002\/pro.4153","article-title":"DichroWeb, a website for calculating protein secondary structure from circular dichroism spectroscopic data","volume":"31","author":"Miles","year":"2022","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102777_bib111","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1006\/abio.2000.4880","article-title":"Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal Biochem."},{"key":"10.1016\/j.jbc.2022.102777_bib112","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J.\u00a0Comput. Chem."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822012200?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822012200?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T20:55:03Z","timestamp":1777409703000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925822012200"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1]]},"references-count":112,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2023,1]]}},"alternative-id":["S0021925822012200"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102777","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2023,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Calmodulin variant E140G associated with long QT syndrome impairs CaMKII\u03b4 autophosphorylation and L-type calcium channel inactivation","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102777","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"102777"}}