Structural Determinants of Oligomerization of the Aquaporin-4 Channel.

The Journal of Biological Chemistry
Philip KitchenAlex C Conner

Abstract

The aquaporin (AQP) family of integral membrane protein channels mediate cellular water and solute flow. Although qualitative and quantitative differences in channel permeability, selectivity, subcellular localization, and trafficking responses have been observed for different members of the AQP family, the signature homotetrameric quaternary structure is conserved. Using a variety of biophysical techniques, we show that mutations to an intracellular loop (loop D) of human AQP4 reduce oligomerization. Non-tetrameric AQP4 mutants are unable to relocalize to the plasma membrane in response to changes in extracellular tonicity, despite equivalent constitutive surface expression levels and water permeability to wild-type AQP4. A network of AQP4 loop D hydrogen bonding interactions, identified using molecular dynamics simulations and based on a comparative mutagenic analysis of AQPs 1, 3, and 4, suggest that loop D interactions may provide a general structural framework for tetrameric assembly within the AQP family.

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Nov 15, 2018·Cells·Marcelo OzuGabriela Amodeo
Jul 10, 2020·PLoS Neglected Tropical Diseases·Juan F QuintanaMark C Field
Nov 7, 2018·Pflügers Archiv : European journal of physiology·Oliver H Wittekindt, Paul Dietl
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Jul 8, 2020·Cells·Claudia D'AgostinoChristine Delporte
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Jan 8, 2020·Genes & Diseases·Shengtao LiaoZhechuan Mei
Jun 28, 2017·ACS Omega·Victoria Schmidt, James N Sturgis

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Methods Mentioned

BETA
transfection
confocal microscopy
transfections
FRET
ELISA
Fluorescence
biosensor
glycosylation
and

Software Mentioned

ImageJ
Matlab
Gromacs
GROMOS
house

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