Molecular characterization of a broad selectivity neutral solute channel

Hiroyasu Tsukaguchi, Chairat Shayakul, Urs V. Berger, Bryan Mackenzie, Sreenivas Devidas, William B. Guggino, Alfred N. Van Hoek, Matthias A. Hediger

Research output: Contribution to journalArticlepeer-review

Abstract

In all living cells, coordination of solute and water movement across cell membranes is of critical importance for osmotic balance. The current concept is that these processes are of distinct biophysical nature. Here we report the expression cloning of a liver cDNA encoding a unique promiscuous solute channel (AQP9) that confers high permeability for both solutes and water. AQP9 mediates passage of a wide variety of non-charged solutes including carbamides, polyols, purines, and pyrimidines in a phloretin- and mercury-sensitive manner, whereas amino acids, cyclic sugars, Na+, K+, Cl- , and deprotonated monocarboxylates are excluded. The properties of AQP9 define a new evolutionary branch of the major intrinsic protein family of aquaporin proteins and describe a previously unknown mechanism by which a large variety of solutes and water can pass through a single pore, enabling rapid cellular uptake or exit of metabolites with minimal osmotic perturbation.

Original languageEnglish (US)
Pages (from-to)24737-24743
Number of pages7
JournalJournal of Biological Chemistry
Volume273
Issue number38
DOIs
StatePublished - Sep 18 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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