AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues

Research output: Contribution to journalJournal articlepeer-review

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AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues. / Assentoft, Mette; Larsen, Brian R; Olesen, Emma T B; Fenton, Robert A; MacAulay, Nanna.

In: American Journal of Physiology: Cell Physiology, Vol. 307, No. 10, 15.11.2014, p. C957-C965.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Assentoft, M, Larsen, BR, Olesen, ETB, Fenton, RA & MacAulay, N 2014, 'AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues', American Journal of Physiology: Cell Physiology, vol. 307, no. 10, pp. C957-C965. https://doi.org/10.1152/ajpcell.00182.2014

APA

Assentoft, M., Larsen, B. R., Olesen, E. T. B., Fenton, R. A., & MacAulay, N. (2014). AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues. American Journal of Physiology: Cell Physiology, 307(10), C957-C965. https://doi.org/10.1152/ajpcell.00182.2014

Vancouver

Assentoft M, Larsen BR, Olesen ETB, Fenton RA, MacAulay N. AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues. American Journal of Physiology: Cell Physiology. 2014 Nov 15;307(10):C957-C965. https://doi.org/10.1152/ajpcell.00182.2014

Author

Assentoft, Mette ; Larsen, Brian R ; Olesen, Emma T B ; Fenton, Robert A ; MacAulay, Nanna. / AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues. In: American Journal of Physiology: Cell Physiology. 2014 ; Vol. 307, No. 10. pp. C957-C965.

Bibtex

@article{5c0d4fca36a345609d5674f1b6070efa,
title = "AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues",
abstract = "Aquaporin 4 (AQP4) is the predominant water channel in the mammalian brain and is mainly expressed in the perivascular glial endfeet at the brain-blood interface. AQP4 serves as a water entry site during brain edema formation, and regulation of AQP4 may therefore be of therapeutic interest. Phosphorylation of aquaporins can regulate plasma membrane localization and, possibly, the unit water permeability via gating of the AQP channel itself. In vivo phosphorylation of six serine residues in the COOH terminus of AQP4 has been detected by mass spectrometry: Ser(276), Ser(285), Ser(315), Ser(316), Ser(321), and Ser(322). To address the role of these phosphorylation sites for AQP4 function, serine-to-alanine mutants were created to abolish the phosphorylation sites. All mutants were detected at the plasma membrane of transfected C6 cells, with the fraction of the total cellular AQP4 expressed at the plasma membrane of transfected C6 cells being similar between the wild-type (WT) and mutant forms of AQP4. Activation of protein kinases A, C, and G in primary astrocytic cultures did not affect the plasma membrane abundance of AQP4. The unit water permeability was determined for the mutant AQP4s upon heterologous expression in Xenopus laevis oocytes (along with serine-to-aspartate mutants of the same residues to mimic a phosphorylation). None of the mutant AQP4 constructs displayed alterations in the unit water permeability. Thus phosphorylation of six different serine residues in the COOH terminus of AQP4 appears not to be required for proper plasma membrane localization of AQP4 or to act as a molecular switch to gate the water channel.",
author = "Mette Assentoft and Larsen, {Brian R} and Olesen, {Emma T B} and Fenton, {Robert A} and Nanna MacAulay",
note = "Copyright {\textcopyright} 2014 the American Physiological Society.",
year = "2014",
month = nov,
day = "15",
doi = "10.1152/ajpcell.00182.2014",
language = "English",
volume = "307",
pages = "C957--C965",
journal = "American Journal of Physiology: Cell Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "10",

}

RIS

TY - JOUR

T1 - AQP4 plasma membrane trafficking or channel gating is not significantly modulated by phosphorylation at COOH-terminal serine residues

AU - Assentoft, Mette

AU - Larsen, Brian R

AU - Olesen, Emma T B

AU - Fenton, Robert A

AU - MacAulay, Nanna

N1 - Copyright © 2014 the American Physiological Society.

PY - 2014/11/15

Y1 - 2014/11/15

N2 - Aquaporin 4 (AQP4) is the predominant water channel in the mammalian brain and is mainly expressed in the perivascular glial endfeet at the brain-blood interface. AQP4 serves as a water entry site during brain edema formation, and regulation of AQP4 may therefore be of therapeutic interest. Phosphorylation of aquaporins can regulate plasma membrane localization and, possibly, the unit water permeability via gating of the AQP channel itself. In vivo phosphorylation of six serine residues in the COOH terminus of AQP4 has been detected by mass spectrometry: Ser(276), Ser(285), Ser(315), Ser(316), Ser(321), and Ser(322). To address the role of these phosphorylation sites for AQP4 function, serine-to-alanine mutants were created to abolish the phosphorylation sites. All mutants were detected at the plasma membrane of transfected C6 cells, with the fraction of the total cellular AQP4 expressed at the plasma membrane of transfected C6 cells being similar between the wild-type (WT) and mutant forms of AQP4. Activation of protein kinases A, C, and G in primary astrocytic cultures did not affect the plasma membrane abundance of AQP4. The unit water permeability was determined for the mutant AQP4s upon heterologous expression in Xenopus laevis oocytes (along with serine-to-aspartate mutants of the same residues to mimic a phosphorylation). None of the mutant AQP4 constructs displayed alterations in the unit water permeability. Thus phosphorylation of six different serine residues in the COOH terminus of AQP4 appears not to be required for proper plasma membrane localization of AQP4 or to act as a molecular switch to gate the water channel.

AB - Aquaporin 4 (AQP4) is the predominant water channel in the mammalian brain and is mainly expressed in the perivascular glial endfeet at the brain-blood interface. AQP4 serves as a water entry site during brain edema formation, and regulation of AQP4 may therefore be of therapeutic interest. Phosphorylation of aquaporins can regulate plasma membrane localization and, possibly, the unit water permeability via gating of the AQP channel itself. In vivo phosphorylation of six serine residues in the COOH terminus of AQP4 has been detected by mass spectrometry: Ser(276), Ser(285), Ser(315), Ser(316), Ser(321), and Ser(322). To address the role of these phosphorylation sites for AQP4 function, serine-to-alanine mutants were created to abolish the phosphorylation sites. All mutants were detected at the plasma membrane of transfected C6 cells, with the fraction of the total cellular AQP4 expressed at the plasma membrane of transfected C6 cells being similar between the wild-type (WT) and mutant forms of AQP4. Activation of protein kinases A, C, and G in primary astrocytic cultures did not affect the plasma membrane abundance of AQP4. The unit water permeability was determined for the mutant AQP4s upon heterologous expression in Xenopus laevis oocytes (along with serine-to-aspartate mutants of the same residues to mimic a phosphorylation). None of the mutant AQP4 constructs displayed alterations in the unit water permeability. Thus phosphorylation of six different serine residues in the COOH terminus of AQP4 appears not to be required for proper plasma membrane localization of AQP4 or to act as a molecular switch to gate the water channel.

U2 - 10.1152/ajpcell.00182.2014

DO - 10.1152/ajpcell.00182.2014

M3 - Journal article

C2 - 25231107

VL - 307

SP - C957-C965

JO - American Journal of Physiology: Cell Physiology

JF - American Journal of Physiology: Cell Physiology

SN - 0363-6143

IS - 10

ER -

ID: 129810371