Control of the Aquaporin‑4 Channel Water Permeability by Structural Dynamics of Aromatic/Arginine Selectivity Filter Residues

The aquaporins (AQPs) make up a family of integral membrane proteins that control cellular water flow. Gating of the water channel by conformational changes induced by phosphorylation or protein–protein interactions is an established regulatory mechanism for AQPs. Recent in silico and crystallograph...

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Bibliographic Details
Published in:Biochemistry (Easton) 2015-11, Vol.54 (45), p.6753-6755
Main Authors: Kitchen, Philip, Conner, Alex C
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Animals
Aquaporin 4 - chemistry
Aquaporin 4 - genetics
Aquaporin 4 - metabolism
Arginine - chemistry
Cell Membrane Permeability - physiology
Dogs
Glycine - chemistry
Histidine - chemistry
Humans
Madin Darby Canine Kidney Cells
Models, Biological
Models, Molecular
Molecular Dynamics Simulation
Mutagenesis, Site-Directed
Protein Conformation
Recombinant Fusion Proteins - metabolism
Structure-Activity Relationship
Transfection
Water - metabolism
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Summary:The aquaporins (AQPs) make up a family of integral membrane proteins that control cellular water flow. Gating of the water channel by conformational changes induced by phosphorylation or protein–protein interactions is an established regulatory mechanism for AQPs. Recent in silico and crystallographic analyses of the structural biology of AQPs suggest that the rate of water flow can also be controlled by small movements of single-amino acid side chains lining the water pore. Here we use measurements of the membrane water permeability of mammalian cells expressing AQP4 mutants to provide the first in vitro evidence in support of this hypothesis.
ISSN:0006-2960
1520-4995
DOI:10.1021/acs.biochem.5b01053