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Updated: Jul 31, 2026

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
Published on: April 20, 2015
Molecular characterization of a broad selectivity neutral solute channel
H Tsukaguchi1, C Shayakul, U V Berger
1Renal Division, Department of Medicine, Brigham & Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
Researchers discovered a new liver protein, aquaporin 9 (AQP9), that transports both water and various solutes across cell membranes. This promiscuous channel protein facilitates metabolite exchange while maintaining osmotic balance, challenging previous concepts of solute and water transport.
Area of Science:
- Cell Biology
- Molecular Biology
- Biophysics
Background:
- Cell membrane transport of solutes and water is crucial for osmotic balance.
- Current understanding posits distinct biophysical mechanisms for solute and water transport.
Purpose of the Study:
- To identify and characterize novel proteins involved in transmembrane transport.
- To elucidate the mechanism of solute and water permeability across cell membranes.
Main Methods:
- Expression cloning of liver cDNA.
- Functional characterization of the cloned protein (AQP9).
- Permeability assays for various solutes and water.
Main Results:
- Identified and cloned aquaporin 9 (AQP9), a liver protein.
- AQP9 exhibits high permeability to water and a wide range of non-charged solutes (e.g., carbamides, polyols, purines, pyrimidines).
- AQP9 is sensitive to phloretin and mercury, excluding charged solutes and certain other molecules.
Conclusions:
- AQP9 represents a new class of aquaporin proteins with promiscuous solute and water transport capabilities.
- This discovery reveals a novel mechanism for simultaneous solute and water passage through a single pore.
- AQP9 enables rapid cellular metabolite exchange with minimal osmotic disruption.
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