Corrigendum to

An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome (Human Mutation, (2015), 36, 8, (764-773), 10.1002/humu.22805)

Marika L. Osterbur, Renjian Zheng, Robert W. Marion, Christine Walsh, Thomas V. McDonald

Research output: Contribution to journalComment/debate

Abstract

An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome Marika L. Osterbur, Renjian Zheng, Robert Marion, Christine Walsh, and Thomas V. McDonald Human Mutation 36; 764–773, 2015 https://doi.org/10.1002/humu.22805 In the above mentioned article published in Human Mutation, the authors characterized a Long QT Syndrome type 2 phenotype due to a c.656A>T (p.Asp219Val) variant in KCNH2. In the original characterization, the authors noted that the p. Asp219Val pathogenic hERG variant caused significant change to the WT hERG electrophysiology and no change in the surface expression of the hERG protein. The authors showed that there was no significant difference in protein expression between the pathogenic variant and the WT protein (Figure 1). The authors also demonstrated that there was no significant difference in current density between the p.Asp219Val hERG variant and the WT hERG variant (Figure 3) and that the p.Asp219Val hERG variant deactivated significantly faster than the WT hERG (Figure 5). The authors now report a correction to these interpretations. Several of the functional effects attributed to this variant appear to be caused by the N-terminal epitope tag and/or an inadvertent PCR mutation present on the mutated hERG protein under study (Osterbur Badhey, Bertalovitz, & McDonald,). In the absence of the N-terminal tag, p.Asp219Val caused a decrease in protein expression and current density. The authors regret their unanticipated technical error published in the original Human Mutation article. Of note, the p.Asp219Val variant reduces effective current to a level of intermediate severity in the untagged version of hERG (Osterbur Badhey et al.,).

Original languageEnglish (US)
Number of pages1
JournalHuman Mutation
Volume40
Issue number3
DOIs
StatePublished - Mar 1 2019

Fingerprint

Long QT Syndrome
Mutation
Proteins
Electrophysiology
Epitopes
Emotions
corrigendum
Phenotype
Polymerase Chain Reaction

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)

Cite this

Corrigendum to : An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome (Human Mutation, (2015), 36, 8, (764-773), 10.1002/humu.22805). / Osterbur, Marika L.; Zheng, Renjian; Marion, Robert W.; Walsh, Christine; McDonald, Thomas V.

In: Human Mutation, Vol. 40, No. 3, 01.03.2019.

Research output: Contribution to journalComment/debate

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abstract = "An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome Marika L. Osterbur, Renjian Zheng, Robert Marion, Christine Walsh, and Thomas V. McDonald Human Mutation 36; 764–773, 2015 https://doi.org/10.1002/humu.22805 In the above mentioned article published in Human Mutation, the authors characterized a Long QT Syndrome type 2 phenotype due to a c.656A>T (p.Asp219Val) variant in KCNH2. In the original characterization, the authors noted that the p. Asp219Val pathogenic hERG variant caused significant change to the WT hERG electrophysiology and no change in the surface expression of the hERG protein. The authors showed that there was no significant difference in protein expression between the pathogenic variant and the WT protein (Figure 1). The authors also demonstrated that there was no significant difference in current density between the p.Asp219Val hERG variant and the WT hERG variant (Figure 3) and that the p.Asp219Val hERG variant deactivated significantly faster than the WT hERG (Figure 5). The authors now report a correction to these interpretations. Several of the functional effects attributed to this variant appear to be caused by the N-terminal epitope tag and/or an inadvertent PCR mutation present on the mutated hERG protein under study (Osterbur Badhey, Bertalovitz, & McDonald,). In the absence of the N-terminal tag, p.Asp219Val caused a decrease in protein expression and current density. The authors regret their unanticipated technical error published in the original Human Mutation article. Of note, the p.Asp219Val variant reduces effective current to a level of intermediate severity in the untagged version of hERG (Osterbur Badhey et al.,).",
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