Novel KLHL26 variant associated with a familial case of Ebstein’s anomaly and left ventricular noncompaction

Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood...

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Vydané v:Molecular genetics & genomic medicine Ročník 8; číslo 4; s. e1152 - n/a
Hlavní autori: Samudrala, Sai Suma K., North, Lauren M., Stamm, Karl D., Earing, Michael G., Frommelt, Michele A., Willes, Richard, Tripathi, Swarnendu, Dsouza, Nikita R., Zimmermann, Michael T., Mahnke, Donna K., Liang, Huan Ling, Lund, Michael, Lin, Chien‐Wei, Geddes, Gabrielle C., Mitchell, Michael E., Tomita‐Mitchell, Aoy
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States John Wiley & Sons, Inc 01.04.2020
John Wiley and Sons Inc
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ISSN:2324-9269, 2324-9269
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Abstract Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC. Methods We performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models. Results Exome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch‐like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC‐affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase. Conclusion In this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin‐mediated protein degradation during cardiac development. Patient's Ebstein's anomaly (EA), a rare congenital heart disease of the tricuspid valve and right ventricle often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Our study identifies a novel, rare, and damaging coding variant c.709C > T (p.R237C) in the Kelch‐like family member 26 (KLHL26) gene with 10 affected out of 17 affected members using Sanger sequencing. Through structural modeling, we show that the KLHL26 variant may affect protein binding to Cullin3 (CUL3), a component of E3 ubiquitin ligase in the ubiquitin‐mediated protein degradation.
AbstractList Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC.BACKGROUNDEbstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC.We performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models.METHODSWe performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models.Exome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch-like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC-affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase.RESULTSExome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch-like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC-affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase.In this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin-mediated protein degradation during cardiac development.CONCLUSIONIn this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin-mediated protein degradation during cardiac development.
Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC. Methods We performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models. Results Exome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch‐like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC‐affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase. Conclusion In this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin‐mediated protein degradation during cardiac development. Patient's Ebstein's anomaly (EA), a rare congenital heart disease of the tricuspid valve and right ventricle often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Our study identifies a novel, rare, and damaging coding variant c.709C > T (p.R237C) in the Kelch‐like family member 26 (KLHL26) gene with 10 affected out of 17 affected members using Sanger sequencing. Through structural modeling, we show that the KLHL26 variant may affect protein binding to Cullin3 (CUL3), a component of E3 ubiquitin ligase in the ubiquitin‐mediated protein degradation.
Abstract Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC. Methods We performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models. Results Exome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch‐like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC‐affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase. Conclusion In this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin‐mediated protein degradation during cardiac development.
Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC. We performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models. Exome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch-like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC-affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase. In this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin-mediated protein degradation during cardiac development.
Patient's Ebstein's anomaly (EA), a rare congenital heart disease of the tricuspid valve and right ventricle often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Our study identifies a novel, rare, and damaging coding variant c.709C > T (p.R237C) in the Kelch‐like family member 26 (KLHL26) gene with 10 affected out of 17 affected members using Sanger sequencing. Through structural modeling, we show that the KLHL26 variant may affect protein binding to Cullin3 (CUL3), a component of E3 ubiquitin ligase in the ubiquitin‐mediated protein degradation.
BackgroundEbstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular noncompaction (LVNC), a cardiomyopathy. Despite implication of cardiac sarcomere genes in some cases, very little is understood regarding the genetic etiology of EA/LVNC. Our study describes a multigenerational family with at least 10 of 17 members affected by EA/LVNC.MethodsWe performed echocardiography on all family members and conducted exome sequencing of six individuals. After identifying candidate variants using two different bioinformatic strategies, we confirmed segregation with phenotype using Sanger sequencing. We investigated structural implications of candidate variants using protein prediction models.ResultsExome sequencing analysis of four affected and two unaffected members identified a novel, rare, and damaging coding variant in the Kelch-like family member 26 (KLHL26) gene located on chromosome 19 at position 237 of the protein (GRCh37). This variant region was confirmed by Sanger sequencing in the remaining family members. KLHL26 (c.709C > T p.R237C) segregates only with EA/LVNC-affected individuals (FBAT p < .05). Investigating structural implications of the candidate variant using protein prediction models suggested that the KLHL26 variant disrupts electrostatic interactions when binding to part of the ubiquitin proteasome, specifically Cullin3 (CUL3), a component of E3 ubiquitin ligase.ConclusionIn this familial case of EA/LVNC, we have identified a candidate gene variant, KLHL26 (p.R237C), which may have an important role in ubiquitin-mediated protein degradation during cardiac development.
Author Frommelt, Michele A.
Geddes, Gabrielle C.
Lin, Chien‐Wei
North, Lauren M.
Dsouza, Nikita R.
Tomita‐Mitchell, Aoy
Mitchell, Michael E.
Stamm, Karl D.
Mahnke, Donna K.
Lund, Michael
Earing, Michael G.
Willes, Richard
Liang, Huan Ling
Tripathi, Swarnendu
Samudrala, Sai Suma K.
Zimmermann, Michael T.
AuthorAffiliation 6 Bioinformatics Research and Developmental Lab Genomic Sciences and Precision Medicine Center Medical College of Wisconsin Milwaukee WI USA
9 Division of Biostatistics Medical College of Wisconsin Milwaukee WI USA
4 Department of Pediatrics Children’s Hospital of Wisconsin Milwaukee WI USA
7 Clinical and Translational Science Institute Medical College of Wisconsin Milwaukee WI USA
10 Department of Biomedical Engineering Medical College of Wisconsin Milwaukee WI USA
3 Department of Surgery Division of Cardiothoracic Surgery Medical College of Wisconsin Milwaukee WI USA
5 Herma Heart Institute Children’s Hospital of Wisconsin Milwaukee WI USA
8 Department of Obstetrics and Gynecology Medical College of Wisconsin Milwaukee WI USA
1 Department of Cell Biology, Neurobiology and Anatomy Medical College of Wisconsin Milwaukee WI USA
2 Department of Otolaryngology and Communication Sciences Medical College of Wisconsin Milwaukee WI USA
AuthorAffiliation_xml – name: 9 Division of Biostatistics Medical College of Wisconsin Milwaukee WI USA
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– name: 6 Bioinformatics Research and Developmental Lab Genomic Sciences and Precision Medicine Center Medical College of Wisconsin Milwaukee WI USA
– name: 10 Department of Biomedical Engineering Medical College of Wisconsin Milwaukee WI USA
– name: 7 Clinical and Translational Science Institute Medical College of Wisconsin Milwaukee WI USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31985165$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1016/j.ejmg.2017.10.003
10.1016/s0378-1119(99)00006-2
10.1016/j.jacc.2017.12.019
10.1371/journal.pone.0165174
10.1002/ajmg.c.31369
10.1371/journal.pone.0118670
10.1016/j.yexcr.2007.12.009
10.1002/ajmg.a.37745
10.1002/ajmg.c.31365
10.1152/ajpcell.00321.2010
10.1038/ng0496-385
10.1038/sj.onc.1203093
10.1016/j.ajhg.2013.10.020
10.1016/j.jacc.2003.10.021
10.1002/ajmg.a.36182
10.1016/j.bbadis.2012.02.007
10.1093/brain/awq108
10.1161/CIRCGENETICS.116.001683
10.1074/jbc.M202596200
10.1016/S1016-8478(23)14020-9
10.1093/nar/gkw304
10.1016/j.ymgme.2004.02.009
10.1016/j.tibs.2004.10.003
10.1074/jbc.RA118.002104
10.1016/j.diff.2013.08.002
10.1002/ajmg.a.34131
10.1371/journal.pone.0001362
10.17116/patol20157763-8
10.1073/pnas.1719309115
10.1161/CIRCULATIONAHA.106.619338
10.1016/j.hfc.2018.02.005
10.1186/gb-2005-6-10-r82
10.1172/JCI8154
10.1891/0730-0832.33.5.268
10.1186/1479-7364-7-13
10.1387/ijdb.113327lp
10.1038/ncb3411
10.1016/j.jcmg.2013.05.021
10.1016/j.ajhg.2010.10.020
10.1016/j.cell.2015.06.043
10.1091/mbc.e03-07-0531
10.1016/j.jmb.2017.02.012
10.1016/j.sbi.2010.08.010
10.1016/j.mod.2009.07.006
10.1161/CIRCGENETICS.110.957985
10.1038/nrm1547
10.1007/s11010-006-9304-6
10.1016/S0021-9258(20)82050-X
10.1002/humu.21302
10.1186/1471-2105-4-42
10.1016/j.molcel.2012.09.018
10.1152/physiolgenomics.00015.2014
10.1016/j.ajhg.2013.05.004
10.1016/j.ijcard.2008.08.035
10.1074/jbc.M112.437996
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Issue 4
Keywords Kelch-like family member 26
left-ventricular noncompaction
Ebstein's anomaly
ubiquitin proteasome
congenital heart defects
Language English
License Attribution
2020 The Authors. Molecular Genetics & Genomic Medicine published by Wiley Periodicals, Inc.
This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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Notes Funding information
This work was supported by National Heart, Lung, and Blood Institute 5T35HL072483‐32 (L.N) and 5T35HL072483‐34 (S.S.), the Wolfe Family Foundation, the Little Hearts for Life Foundation, the Medical College of Wisconsin's Department of Surgery, and the Children's Hospital of Wisconsin Research Institute. S.S. is a member of the Medical Scientist Training Program at MCW, which is partially supported by a training grant from National Institute of General Medical Sciences T32‐GM080202.
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References 2004; 29
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2018; 293
1999; 18
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2008; 26
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2008; 314
2007; 2
2018; 71
2014; 7
2003; 42
2009; 126
2016; 44
2015; 162
1983; 258
2010; 31
2004; 82
2012; 1822
2013; 86
2015; 10
2013; 93
2014; 46
2018; 61
2013; 163C
2016; 18
2011; 4
1999; 228
1999; 104
1996; 12
2016; 11
2007; 115
2017; 429
2010; 87
2011; 300
2010; 138
2004; 15
2017; 10
2018; 115
2010; 133
2005; 6
2012; 48
2016; 170
2014; 33
2018; 14
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References_xml – volume: 14
  start-page: 283
  issue: 3
  year: 2018
  end-page: 295
  article-title: Right heart‐pulmonary circulation unit in congenital heart diseases
  publication-title: Heart Failure Clinics
– volume: 288
  start-page: 7803
  issue: 11
  year: 2013
  end-page: 7814
  article-title: Structural basis for Cul3 protein assembly with the BTB‐Kelch family of E3 ubiquitin ligases
  publication-title: Journal of Biological Chemistry
– volume: 15
  start-page: 1172
  issue: 3
  year: 2004
  end-page: 1184
  article-title: Novel kelch‐like protein, KLEIP, is involved in actin assembly at cell‐cell contact sites of Madin‐Darby canine kidney cells
  publication-title: Molecular Biology of the Cell
– volume: 18
  start-page: 6829
  issue: 48
  year: 1999
  end-page: 6834
  article-title: Covalent modification of all members of human cullin family proteins by NEDD8
  publication-title: Oncogene
– volume: 228
  start-page: 73
  issue: 1–2
  year: 1999
  end-page: 83
  article-title: Isolation and characterization of IPP, a novel human gene encoding an actin‐binding, kelch‐like protein
  publication-title: Gene
– volume: 71
  start-page: 711
  issue: 7
  year: 2018
  end-page: 722
  article-title: Genetics, clinical features, and long‐term outcome of noncompaction cardiomyopathy
  publication-title: Journal of the American College of Cardiology
– volume: 138
  start-page: 261
  issue: 3
  year: 2010
  end-page: 265
  article-title: NKX2.5 mutations in patients with non‐syndromic congenital heart disease
  publication-title: International Journal of Cardiology
– volume: 10
  issue: 6
  year: 2017
  article-title: Familial Ebstein anomaly: Whole exome sequencing identifies novel phenotype associated with FLNA
  publication-title: Circulation: Cardiovascular Genetics
– volume: 314
  start-page: 1177
  issue: 5
  year: 2008
  end-page: 1191
  article-title: Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes
  publication-title: Experimental Cell Research
– volume: 161A
  start-page: 3187
  issue: 12
  year: 2013
  end-page: 3190
  article-title: Familial ebstein anomaly, left ventricular hypertrabeculation, and ventricular septal defect associated with a MYH7 mutation
  publication-title: American Journal of Medical Genetics. Part A
– volume: 6
  start-page: R82
  issue: 10
  year: 2005
  article-title: Sequence and structural analysis of BTB domain proteins
  publication-title: Genome Biology
– volume: 86
  start-page: 184
  issue: 4–5
  year: 2013
  end-page: 191
  article-title: Kbtbd5 is regulated by MyoD and restricted to the myogenic lineage
  publication-title: Differentiation
– volume: 11
  issue: 10
  year: 2016
  article-title: Genetic variants in isolated Ebstein anomaly implicated in myocardial development pathways
  publication-title: PLoS ONE
– volume: 4
  start-page: 43
  issue: 1
  year: 2011
  end-page: 50
  article-title: Mutations in the sarcomere gene MYH7 in Ebstein anomaly
  publication-title: Circulation: Cardiovascular Genetics
– volume: 293
  start-page: 8802
  issue: 23
  year: 2018
  end-page: 8811
  article-title: Cullin‐3‐RING ubiquitin ligase activity is required for striated muscle function in mice
  publication-title: Journal of Biological Chemistry
– volume: 163C
  start-page: 178
  issue: 3
  year: 2013
  end-page: 184
  article-title: Ebstein anomaly associated with left ventricular noncompaction: An autosomal dominant condition that can be caused by mutations in MYH7
  publication-title: American Journal of Medical Genetics Part C: Seminars in Medical Genetics
– volume: 115
  start-page: 277
  issue: 2
  year: 2007
  end-page: 285
  article-title: Ebstein's anomaly
  publication-title: Circulation
– volume: 296
  start-page: 109
  issue: 1–2
  year: 2007
  end-page: 119
  article-title: Differential subcellular localization and activity of kelch repeat proteins KLHDC1 and KLHDC2
  publication-title: Molecular and Cellular Biochemistry
– volume: 42
  start-page: 2014
  issue: 11
  year: 2003
  end-page: 2027
  article-title: Mutations in Cypher/ZASP in patients with dilated cardiomyopathy and left ventricular non‐compaction
  publication-title: Journal of the American College of Cardiology
– volume: 7
  start-page: 207
  issue: 2
  year: 2014
  end-page: 209
  article-title: LV Noncompaction in Ebstein's anomaly in infants and outcomes
  publication-title: JACC: Cardiovascular Imaging
– volume: 31
  start-page: E1609
  issue: 8
  year: 2010
  end-page: 1621
  article-title: A homozygous SCN5A mutation in a severe, recessive type of cardiac conduction disease
  publication-title: Human Mutation
– volume: 48
  start-page: 692
  issue: 5
  year: 2012
  end-page: 704
  article-title: The Kelch repeat protein KLHDC10 regulates oxidative stress‐induced ASK1 activation by suppressing PP5
  publication-title: Molecular Cell
– volume: 429
  start-page: 1045
  issue: 7
  year: 2017
  end-page: 1066
  article-title: Cullin E3 ligase activity is required for myoblast differentiation
  publication-title: Journal of Molecular Biology
– volume: 104
  start-page: 1567
  issue: 11
  year: 1999
  end-page: 1573
  article-title: Mutations in the cardiac transcription factor NKX2.5 affect diverse cardiac developmental pathways
  publication-title: Journal of Clinical Investigation
– volume: 277
  start-page: 44140
  issue: 46
  year: 2002
  end-page: 44146
  article-title: Identification of Nd1, a novel murine kelch family protein, involved in stabilization of actin filaments
  publication-title: Journal of Biological Chemistry
– volume: 20
  start-page: 714
  issue: 6
  year: 2010
  end-page: 721
  article-title: Structural assembly of cullin‐RING ubiquitin ligase complexes
  publication-title: Current Opinion in Structural Biology
– volume: 170
  start-page: 2186
  issue: 8
  year: 2016
  end-page: 2190
  article-title: Ebstein anomaly, left ventricular non‐compaction, and early onset heart failure associated with a de novo alpha‐tropomyosin gene mutation
  publication-title: American Journal of Medical Genetics. Part A
– volume: 46
  start-page: 482
  issue: 13
  year: 2014
  end-page: 495
  article-title: Transcriptional atlas of cardiogenesis maps congenital heart disease interactome
  publication-title: Physiological Genomics
– volume: 12
  start-page: 385
  issue: 4
  year: 1996
  end-page: 389
  article-title: A novel X‐linked gene, G4.5. is responsible for Barth syndrome
  publication-title: Nature Genetics
– volume: 56
  start-page: 301
  issue: 4
  year: 2012
  end-page: 309
  article-title: Sarcosin (Krp1) in skeletal muscle differentiation: Gene expression profiling and knockdown experiments
  publication-title: International Journal of Developmental Biology
– volume: 258
  start-page: 8206
  issue: 13
  year: 1983
  end-page: 8214
  article-title: Components of ubiquitin‐protein ligase system. Resolution, affinity purification, and role in protein breakdown
  publication-title: Journal of Biological Chemistry
– volume: 163C
  start-page: 144
  issue: 3
  year: 2013
  end-page: 156
  article-title: Molecular mechanism of ventricular trabeculation/compaction and the pathogenesis of the left ventricular noncompaction cardiomyopathy (LVNC)
  publication-title: American Journal of Medical Genetics Part C: Seminars in Medical Genetics
– volume: 115
  start-page: E4101
  issue: 17
  year: 2018
  end-page: E4110
  article-title: Neddylation mediates ventricular chamber maturation through repression of Hippo signaling
  publication-title: Proceedings of the National Academy of Sciences of the United States of America
– volume: 4
  start-page: 42
  year: 2003
  article-title: Molecular phylogeny of the kelch‐repeat superfamily reveals an expansion of BTB/kelch proteins in animals
  publication-title: BMC Bioinformatics
– volume: 300
  start-page: C1345
  issue: 6
  year: 2011
  end-page: 1355
  article-title: BTB‐Kelch protein Krp1 regulates proliferation and differentiation of myoblasts
  publication-title: American Journal of Physiology. Cell Physiology
– volume: 44
  start-page: W356
  issue: W1
  year: 2016
  end-page: 360
  article-title: Protein Frustratometer 2: A tool to localize energetic frustration in protein molecules, now with electrostatics
  publication-title: Nucleic Acids Research
– volume: 93
  start-page: 1108
  issue: 6
  year: 2013
  end-page: 1117
  article-title: Identification of KLHL41 mutations implicates BTB‐Kelch‐mediated ubiquitination as an alternate pathway to myofibrillar disruption in nemaline myopathy
  publication-title: American Journal of Human Genetics
– volume: 6
  start-page: 9
  issue: 1
  year: 2005
  end-page: 20
  article-title: Function and regulation of cullin‐RING ubiquitin ligases
  publication-title: Nature Reviews Molecular Cell Biology
– volume: 126
  start-page: 852
  issue: 10
  year: 2009
  end-page: 862
  article-title: Klhl31 is associated with skeletal myogenesis and its expression is regulated by myogenic signals and Myf‐5
  publication-title: Mechanisms of Development
– volume: 93
  start-page: 6
  issue: 1
  year: 2013
  end-page: 18
  article-title: Mutations in KLHL40 are a frequent cause of severe autosomal‐recessive nemaline myopathy
  publication-title: American Journal of Human Genetics
– volume: 77
  start-page: 3
  issue: 6
  year: 2015
  end-page: 8
  article-title: Altered Z‐disks of myofibrils in the cardiomyocytes from patients with Ebstein's anomaly
  publication-title: Arkhiv Patologii
– volume: 29
  start-page: 634
  issue: 12
  year: 2004
  end-page: 637
  article-title: The BACK domain in BTB‐kelch proteins
  publication-title: Trends in Biochemical Sciences
– volume: 10
  issue: 2
  year: 2015
  article-title: Activin‐A and Bmp4 levels modulate cell type specification during CHIR‐induced cardiomyogenesis
  publication-title: PLoS ONE
– volume: 155A
  start-page: 2196
  issue: 9
  year: 2011
  end-page: 2202
  article-title: Ebstein anomaly: Genetic heterogeneity and association with microdeletions 1p36 and 8p23.1
  publication-title: American Journal of Medical Genetics. Part A
– volume: 7
  start-page: 13
  year: 2013
  article-title: Update on the Kelch‐like (KLHL) gene family
  publication-title: Hum Genomics
– volume: 18
  start-page: 1031
  issue: 10
  year: 2016
  end-page: 1042
  article-title: iPSC‐derived cardiomyocytes reveal abnormal TGF‐beta signalling in left ventricular non‐compaction cardiomyopathy
  publication-title: Nature Cell Biology
– volume: 26
  start-page: 443
  issue: 5
  year: 2008
  end-page: 453
  article-title: A novel human BTB‐kelch protein KLHL31, strongly expressed in muscle and heart, inhibits transcriptional activities of TRE and SRE
  publication-title: Molecules and Cells
– volume: 1822
  start-page: 1038
  issue: 6
  year: 2012
  end-page: 1050
  article-title: Disruption of Nrf2/ARE signaling impairs antioxidant mechanisms and promotes cell degradation pathways in aged skeletal muscle
  publication-title: Biochimica Et Biophysica Acta
– volume: 133
  start-page: 2123
  issue: 7
  year: 2010
  end-page: 2135
  article-title: Kelch‐like homologue 9 mutation is associated with an early onset autosomal dominant distal myopathy
  publication-title: Brain
– volume: 2
  issue: 12
  year: 2007
  article-title: Noncompaction of the ventricular myocardium is associated with a de novo mutation in the beta‐myosin heavy chain gene
  publication-title: PLoS ONE
– volume: 82
  start-page: 162
  issue: 2
  year: 2004
  end-page: 166
  article-title: Isolated left ventricular noncompaction is rarely caused by mutations in G4.5, alpha‐dystrobrevin and FK Binding Protein‐12
  publication-title: Molecular Genetics and Metabolism
– volume: 87
  start-page: 842
  issue: 6
  year: 2010
  end-page: 847
  article-title: Dominant mutations in KBTBD13, a member of the BTB/Kelch family, cause nemaline myopathy with cores
  publication-title: American Journal of Human Genetics
– volume: 33
  start-page: 268
  issue: 5
  year: 2014
  end-page: 274
  article-title: Ebstein anomaly: A review
  publication-title: Neonatal Network
– volume: 61
  start-page: 8
  issue: 1
  year: 2018
  end-page: 10
  article-title: Left ventricular non‐compaction with Ebstein anomaly attributed to a TPM1 mutation
  publication-title: European Journal of Medical Genetics
– volume: 162
  start-page: 425
  issue: 2
  year: 2015
  end-page: 440
  article-title: The BioPlex Network: A Systematic exploration of the human interactome
  publication-title: Cell
– ident: e_1_2_8_34_1
  doi: 10.1016/j.ejmg.2017.10.003
– ident: e_1_2_8_27_1
  doi: 10.1016/s0378-1119(99)00006-2
– ident: e_1_2_8_49_1
  doi: 10.1016/j.jacc.2017.12.019
– ident: e_1_2_8_46_1
  doi: 10.1371/journal.pone.0165174
– ident: e_1_2_8_54_1
  doi: 10.1002/ajmg.c.31369
– ident: e_1_2_8_28_1
  doi: 10.1371/journal.pone.0118670
– ident: e_1_2_8_19_1
  doi: 10.1016/j.yexcr.2007.12.009
– ident: e_1_2_8_25_1
  doi: 10.1002/ajmg.a.37745
– ident: e_1_2_8_51_1
  doi: 10.1002/ajmg.c.31365
– ident: e_1_2_8_37_1
  doi: 10.1152/ajpcell.00321.2010
– ident: e_1_2_8_6_1
  doi: 10.1038/ng0496-385
– ident: e_1_2_8_23_1
  doi: 10.1038/sj.onc.1203093
– ident: e_1_2_8_20_1
  doi: 10.1016/j.ajhg.2013.10.020
– ident: e_1_2_8_50_1
  doi: 10.1016/j.jacc.2003.10.021
– ident: e_1_2_8_5_1
  doi: 10.1002/ajmg.a.36182
– ident: e_1_2_8_32_1
  doi: 10.1016/j.bbadis.2012.02.007
– ident: e_1_2_8_12_1
  doi: 10.1093/brain/awq108
– ident: e_1_2_8_31_1
  doi: 10.1161/CIRCGENETICS.116.001683
– ident: e_1_2_8_44_1
  doi: 10.1074/jbc.M202596200
– ident: e_1_2_8_53_1
  doi: 10.1016/S1016-8478(23)14020-9
– ident: e_1_2_8_36_1
  doi: 10.1093/nar/gkw304
– ident: e_1_2_8_26_1
  doi: 10.1016/j.ymgme.2004.02.009
– ident: e_1_2_8_48_1
  doi: 10.1016/j.tibs.2004.10.003
– ident: e_1_2_8_35_1
  doi: 10.1074/jbc.RA118.002104
– ident: e_1_2_8_8_1
  doi: 10.1016/j.diff.2013.08.002
– ident: e_1_2_8_14_1
  doi: 10.1002/ajmg.a.34131
– ident: e_1_2_8_9_1
  doi: 10.1371/journal.pone.0001362
– ident: e_1_2_8_16_1
  doi: 10.17116/patol20157763-8
– ident: e_1_2_8_56_1
  doi: 10.1073/pnas.1719309115
– ident: e_1_2_8_3_1
  doi: 10.1161/CIRCULATIONAHA.106.619338
– ident: e_1_2_8_52_1
  doi: 10.1016/j.hfc.2018.02.005
– ident: e_1_2_8_47_1
  doi: 10.1186/gb-2005-6-10-r82
– ident: e_1_2_8_4_1
  doi: 10.1172/JCI8154
– ident: e_1_2_8_17_1
  doi: 10.1891/0730-0832.33.5.268
– ident: e_1_2_8_13_1
  doi: 10.1186/1479-7364-7-13
– ident: e_1_2_8_15_1
  doi: 10.1387/ijdb.113327lp
– ident: e_1_2_8_29_1
  doi: 10.1038/ncb3411
– ident: e_1_2_8_39_1
  doi: 10.1016/j.jcmg.2013.05.021
– ident: e_1_2_8_43_1
  doi: 10.1016/j.ajhg.2010.10.020
– ident: e_1_2_8_24_1
  doi: 10.1016/j.cell.2015.06.043
– ident: e_1_2_8_21_1
  doi: 10.1091/mbc.e03-07-0531
– ident: e_1_2_8_7_1
  doi: 10.1016/j.jmb.2017.02.012
– ident: e_1_2_8_55_1
  doi: 10.1016/j.sbi.2010.08.010
– ident: e_1_2_8_2_1
  doi: 10.1016/j.mod.2009.07.006
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  doi: 10.1161/CIRCGENETICS.110.957985
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  doi: 10.1038/nrm1547
– ident: e_1_2_8_11_1
  doi: 10.1007/s11010-006-9304-6
– ident: e_1_2_8_22_1
  doi: 10.1016/S0021-9258(20)82050-X
– ident: e_1_2_8_33_1
  doi: 10.1002/humu.21302
– ident: e_1_2_8_41_1
  doi: 10.1186/1471-2105-4-42
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  doi: 10.1016/j.molcel.2012.09.018
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  doi: 10.1152/physiolgenomics.00015.2014
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  doi: 10.1016/j.ajhg.2013.05.004
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Snippet Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left...
Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left ventricular...
BackgroundEbstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with left...
Patient's Ebstein's anomaly (EA), a rare congenital heart disease of the tricuspid valve and right ventricle often manifest with left ventricular noncompaction...
Abstract Background Ebstein's anomaly (EA) is a rare congenital heart disease of the tricuspid valve and right ventricle. Patients with EA often manifest with...
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StartPage e1152
SubjectTerms Adult
Age
Binding Sites
Biodegradation
Cardiomyopathy
Cardiovascular diseases
Child
Child, Preschool
Children & youth
Chromosome 19
Chromosomes
congenital heart defects
Coronary artery disease
Cullin Proteins - metabolism
Ebstein Anomaly - genetics
Ebstein Anomaly - pathology
Ebstein's anomaly
Echocardiography
Electrostatic properties
Etiology
Families & family life
Female
Genes
Genetic Testing
Heart Defects, Congenital - genetics
Heart Defects, Congenital - pathology
Heart diseases
Humans
Infant, Newborn
Kelch‐like family member 26
left‐ventricular noncompaction
Loss of Function Mutation
Male
Middle Aged
Original
Pedigree
Phenotypes
Prediction models
Premature birth
Proteasomes
Protein Binding
Proteins
Rheumatic heart disease
Sequence analysis
Transcription factors
Tricuspid valve
Ubiquitin
ubiquitin proteasome
Ubiquitin-protein ligase
Ventricle
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Title Novel KLHL26 variant associated with a familial case of Ebstein’s anomaly and left ventricular noncompaction
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