Structure, function and translational relevance of aquaporin dual water and ion channels

A. J. Yool, E. M. Campbell

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

Aquaporins have been assumed to be selective for water alone, and aquaglyceroporins are accepted as carrying water and small uncharged solutes including glycerol. This review presents an expanded view of aquaporins as channels with more complex mechanisms of regulation and diverse repertoires of substrate permeabilities than were originally appreciated in the early establishment of the field. The role of aquaporins as dual water and gated ion channels is likely to have physiological and potentially translational relevance, and can be evaluated with newly developed molecular and pharmacological tools. Ion channel activity has been shown for Aquaporins -0, -1, and -6, Drosphila Big Brain, and plant Nodulin-26. Although the concept of ion channel function in aquaporins remains controversial, research advances are beginning to define not only the ion channel function but also the detailed molecular mechanisms that govern and mediate the multifunctional capabilities. With regard to physiological relevance, the adaptive benefit of expression of ion channel activity in aquaporins, implied by amino acid sequence conservation of the ion channel gating domains, suggests they provide more than water or glycerol and solute transport. Dual ion and water channels are of interest for understanding the modulation of transmembrane fluid gradients, volume regulation, and possible signal transduction in tissues expressing classes of aquaporins that have the dual function capability. Other aquaporin classes might be found in future work to have ion channel activities, pending identification of the possible signaling pathways that could govern activation.
Original languageEnglish
Pages (from-to)553-561
Number of pages9
JournalMolecular Aspects of Medicine
Volume33
Issue number5-6
DOIs
Publication statusPublished - Oct 2012

Fingerprint

Aquaporins
Ion Channels
Water
Glycerol
Aquaglyceroporins
Ion Channel Gating
Aquaporin 1
Solute transport
Signal transduction
Amino Acid Sequence
Permeability
Signal Transduction
Conservation
Brain
Chemical activation
Modulation
Pharmacology
Tissue
Amino Acids
Fluids

Keywords

  • MIP
  • arylsulfonamide
  • nonselective cation channel
  • cyclic GMP
  • AQP
  • fluid transport

Cite this

Structure, function and translational relevance of aquaporin dual water and ion channels. / Yool, A. J.; Campbell, E. M.

In: Molecular Aspects of Medicine, Vol. 33, No. 5-6, 10.2012, p. 553-561.

Research output: Contribution to journalArticle

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