The novel C-terminal KCNQ1 mutation M520R alters protein trafficking.

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The novel C-terminal KCNQ1 mutation M520R alters protein trafficking. / Schmitt, Nicole; Calloe, Kirstine; Nielsen, Nathalie Hélix; Buschmann, Maria; Speckmann, Erwin-Josef; Schulze-Bahr, Eric; Schwarz, Martin.

In: Biochemical and Biophysical Research Communications, Vol. 358, No. 1, 2007, p. 304-10.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schmitt, N, Calloe, K, Nielsen, NH, Buschmann, M, Speckmann, E-J, Schulze-Bahr, E & Schwarz, M 2007, 'The novel C-terminal KCNQ1 mutation M520R alters protein trafficking.', Biochemical and Biophysical Research Communications, vol. 358, no. 1, pp. 304-10. https://doi.org/10.1016/j.bbrc.2007.04.127

APA

Schmitt, N., Calloe, K., Nielsen, N. H., Buschmann, M., Speckmann, E-J., Schulze-Bahr, E., & Schwarz, M. (2007). The novel C-terminal KCNQ1 mutation M520R alters protein trafficking. Biochemical and Biophysical Research Communications, 358(1), 304-10. https://doi.org/10.1016/j.bbrc.2007.04.127

Vancouver

Schmitt N, Calloe K, Nielsen NH, Buschmann M, Speckmann E-J, Schulze-Bahr E et al. The novel C-terminal KCNQ1 mutation M520R alters protein trafficking. Biochemical and Biophysical Research Communications. 2007;358(1):304-10. https://doi.org/10.1016/j.bbrc.2007.04.127

Author

Schmitt, Nicole ; Calloe, Kirstine ; Nielsen, Nathalie Hélix ; Buschmann, Maria ; Speckmann, Erwin-Josef ; Schulze-Bahr, Eric ; Schwarz, Martin. / The novel C-terminal KCNQ1 mutation M520R alters protein trafficking. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 358, No. 1. pp. 304-10.

Bibtex

@article{9a98fe70e92211dcbee902004c4f4f50,

title = "The novel C-terminal KCNQ1 mutation M520R alters protein trafficking.",

abstract = "The long QT-syndrome is characterized by a prolongation of the QT-interval and tachyarrhythmias causing syncopes and sudden death. We identified the missense mutation M520R in the calmodulin binding domain of the Kv7.1 channel from a German family with long QT-syndrome. Heterologous expression of the mutant did not reveal any whole-cell currents independent of the auxiliary subunit KCNE1. Co-expression of the wild-type Kv7.1 channels and the mutant showed that the mutant did not have a dominant negative effect. In immunocytochemical assays of transfected COS-1 cells wild-type Kv7.1 showed an immunopositive labeling of the plasma membrane. For M520R no plasma membrane staining was visible, instead a strong signal in the ER was observed. These results indicate that the LQT1 mutation M520R leads to ER-retention and dysfunctional trafficking of the mutant channel resulting in haploinsufficiency. Udgivelsesdato: 2007-Jun-22",

author = "Nicole Schmitt and Kirstine Calloe and Nielsen, {Nathalie H{\'e}lix} and Maria Buschmann and Erwin-Josef Speckmann and Eric Schulze-Bahr and Martin Schwarz",

note = "Keywords: Adult; Amino Acid Sequence; Animals; CHO Cells; COS Cells; Cell Membrane; Cercopithecus aethiops; Cricetinae; Cricetulus; Endoplasmic Reticulum; Female; Humans; KCNQ1 Potassium Channel; Long QT Syndrome; Middle Aged; Molecular Sequence Data; Mutation, Missense; Patch-Clamp Techniques; Pedigree; Protein Structure, Tertiary; Protein Transport",

year = "2007",

doi = "10.1016/j.bbrc.2007.04.127",

language = "English",

volume = "358",

pages = "304--10",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "1",

}

RIS

TY - JOUR

T1 - The novel C-terminal KCNQ1 mutation M520R alters protein trafficking.

AU - Schmitt, Nicole

AU - Calloe, Kirstine

AU - Nielsen, Nathalie Hélix

AU - Buschmann, Maria

AU - Speckmann, Erwin-Josef

AU - Schulze-Bahr, Eric

AU - Schwarz, Martin

N1 - Keywords: Adult; Amino Acid Sequence; Animals; CHO Cells; COS Cells; Cell Membrane; Cercopithecus aethiops; Cricetinae; Cricetulus; Endoplasmic Reticulum; Female; Humans; KCNQ1 Potassium Channel; Long QT Syndrome; Middle Aged; Molecular Sequence Data; Mutation, Missense; Patch-Clamp Techniques; Pedigree; Protein Structure, Tertiary; Protein Transport

PY - 2007

Y1 - 2007

N2 - The long QT-syndrome is characterized by a prolongation of the QT-interval and tachyarrhythmias causing syncopes and sudden death. We identified the missense mutation M520R in the calmodulin binding domain of the Kv7.1 channel from a German family with long QT-syndrome. Heterologous expression of the mutant did not reveal any whole-cell currents independent of the auxiliary subunit KCNE1. Co-expression of the wild-type Kv7.1 channels and the mutant showed that the mutant did not have a dominant negative effect. In immunocytochemical assays of transfected COS-1 cells wild-type Kv7.1 showed an immunopositive labeling of the plasma membrane. For M520R no plasma membrane staining was visible, instead a strong signal in the ER was observed. These results indicate that the LQT1 mutation M520R leads to ER-retention and dysfunctional trafficking of the mutant channel resulting in haploinsufficiency. Udgivelsesdato: 2007-Jun-22

AB - The long QT-syndrome is characterized by a prolongation of the QT-interval and tachyarrhythmias causing syncopes and sudden death. We identified the missense mutation M520R in the calmodulin binding domain of the Kv7.1 channel from a German family with long QT-syndrome. Heterologous expression of the mutant did not reveal any whole-cell currents independent of the auxiliary subunit KCNE1. Co-expression of the wild-type Kv7.1 channels and the mutant showed that the mutant did not have a dominant negative effect. In immunocytochemical assays of transfected COS-1 cells wild-type Kv7.1 showed an immunopositive labeling of the plasma membrane. For M520R no plasma membrane staining was visible, instead a strong signal in the ER was observed. These results indicate that the LQT1 mutation M520R leads to ER-retention and dysfunctional trafficking of the mutant channel resulting in haploinsufficiency. Udgivelsesdato: 2007-Jun-22

U2 - 10.1016/j.bbrc.2007.04.127

DO - 10.1016/j.bbrc.2007.04.127

M3 - Journal article

C2 - 17482572

VL - 358

SP - 304

EP - 310

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -

ID: 2983028