Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit

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

Standard

Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit. / Vestergaard, Anna L.; Mikkelsen, Stine A.; Coleman, Jonathan A.; Molday, Robert S.; Vilsen, Bente; Andersen, Jens Peter.

In: F E B S Letters, Vol. 589, No. 24, Part B, 2015, p. 3908-3914.

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

Harvard

Vestergaard, AL, Mikkelsen, SA, Coleman, JA, Molday, RS, Vilsen, B & Andersen, JP 2015, 'Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit', F E B S Letters, vol. 589, no. 24, Part B, pp. 3908-3914. https://doi.org/10.1016/j.febslet.2015.11.031

APA

Vestergaard, A. L., Mikkelsen, S. A., Coleman, J. A., Molday, R. S., Vilsen, B., & Andersen, J. P. (2015). Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit. F E B S Letters, 589(24, Part B), 3908-3914. https://doi.org/10.1016/j.febslet.2015.11.031

Vancouver

Vestergaard AL, Mikkelsen SA, Coleman JA, Molday RS, Vilsen B, Andersen JP. Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit. F E B S Letters. 2015;589(24, Part B):3908-3914. https://doi.org/10.1016/j.febslet.2015.11.031

Author

Vestergaard, Anna L. ; Mikkelsen, Stine A. ; Coleman, Jonathan A. ; Molday, Robert S. ; Vilsen, Bente ; Andersen, Jens Peter. / Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit. In: F E B S Letters. 2015 ; Vol. 589, No. 24, Part B. pp. 3908-3914.

Bibtex

@article{297e752f037b40b197378fc805b7bb8a,
title = "Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit",
abstract = "P4-ATPases, or flippases, translocate phospholipids between the two leaflets of eukaryotic biological membranes. They are essential to the physiologically crucial phospholipid asymmetry and involved in severe diseases, but their molecular structure and mechanism are still unresolved. Here, we show that in an extensive mutational alanine screening of the mammalian flippase ATP8A2 catalytic subunit, five mutations stand out by leading to reduced glycosylation of the accessory subunit CDC50A. These mutations may disturb the interaction between the subunits.",
author = "Vestergaard, {Anna L.} and Mikkelsen, {Stine A.} and Coleman, {Jonathan A.} and Molday, {Robert S.} and Bente Vilsen and Andersen, {Jens Peter}",
year = "2015",
doi = "10.1016/j.febslet.2015.11.031",
language = "English",
volume = "589",
pages = "3908--3914",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "24, Part B",

}

RIS

TY - JOUR

T1 - Specific Mutations in Mammalian P4-ATPase ATP8A2 Catalytic Subunit Entail Differential Glycosylation of the Accessory CDC50A Subunit

AU - Vestergaard, Anna L.

AU - Mikkelsen, Stine A.

AU - Coleman, Jonathan A.

AU - Molday, Robert S.

AU - Vilsen, Bente

AU - Andersen, Jens Peter

PY - 2015

Y1 - 2015

N2 - P4-ATPases, or flippases, translocate phospholipids between the two leaflets of eukaryotic biological membranes. They are essential to the physiologically crucial phospholipid asymmetry and involved in severe diseases, but their molecular structure and mechanism are still unresolved. Here, we show that in an extensive mutational alanine screening of the mammalian flippase ATP8A2 catalytic subunit, five mutations stand out by leading to reduced glycosylation of the accessory subunit CDC50A. These mutations may disturb the interaction between the subunits.

AB - P4-ATPases, or flippases, translocate phospholipids between the two leaflets of eukaryotic biological membranes. They are essential to the physiologically crucial phospholipid asymmetry and involved in severe diseases, but their molecular structure and mechanism are still unresolved. Here, we show that in an extensive mutational alanine screening of the mammalian flippase ATP8A2 catalytic subunit, five mutations stand out by leading to reduced glycosylation of the accessory subunit CDC50A. These mutations may disturb the interaction between the subunits.

U2 - 10.1016/j.febslet.2015.11.031

DO - 10.1016/j.febslet.2015.11.031

M3 - Journal article

C2 - 26592152

VL - 589

SP - 3908

EP - 3914

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 24, Part B

ER -

ID: 147984684