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  Phosphorylation of rat aquaporin-4 at Ser111 is not required for channel gating.

Assentoft, M., Kaptan, S., Fenton, R. A., Hua, S. Z., de Groot, B. L., & MacAulay, N. (2013). Phosphorylation of rat aquaporin-4 at Ser111 is not required for channel gating. Glia, 61(7), 1101-1112. doi:10.1002/glia.22498.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-FD50-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CA5A-0
Genre: Journal Article

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Assentoft, M., Author
Kaptan, S.1, Author              
Fenton, R. A., Author
Hua, S. Z., Author
de Groot, B. L.1, Author              
MacAulay, N., Author
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1Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578573              

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 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 has been described as an important entry and exit site for water during formation of brain edema and regulation of AQP4 is therefore of therapeutic interest. Phosphorylation of some aquaporins has been proposed to regulate their water permeability via gating of the channel itself. Protein kinase (PK)-dependent phosphorylation of Ser111 has been reported to increase the water permeability of AQP4 expressed in an astrocytic cell line. This possibility was, however, questioned based on the crystal structure of the human AQP4. Our study aimed to resolve if Ser111 was indeed a site involved in phosphorylation-mediated gating of AQP4. The water permeability of AQP4-expressing Xenopus oocytes was not altered by a range of activators and inhibitors of PKG and PKA. Mutation of Ser111 to alanine or aspartate (to prevent or mimic phosphorylation) did not change the water permeability of AQP4. PKG activation had no effect on the water permeability of AQP4 in primary cultures of rat astrocytes. Molecular dynamics simulations of a phosphorylation of AQP4.Ser111 recorded no phosphorylation-induced change in water permeability. A phospho-specific antibody, exclusively recognizing AQP4 when phosphorylated on Ser111, failed to detect phosphorylation in cell lysate of rat brain stimulated by conditions proposed to induce phosphorylation of this residue. Thus, our data indicate a lack of phosphorylation of Ser111 and of phosphorylation-dependent gating of AQP4.

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Language(s): eng - English
 Dates: 2013-04-252013-07
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/glia.22498
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Title: Glia
Source Genre: Journal
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Pages: - Volume / Issue: 61 (7) Sequence Number: - Start / End Page: 1101 - 1112 Identifier: -