FEBS Letters
Volume 584, Issue 12 , Pages 2580-2588, 18 June 2010

Structural insights into eukaryotic aquaporin regulation

Edited by Jan Rydström

  • Susanna Törnroth-Horsefield

      Affiliations

    • Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden
    • ,
  • Kristina Hedfalk

      Affiliations

    • Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden
    • ,
  • Gerhard Fischer

      Affiliations

    • Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden
    • ,
  • Karin Lindkvist-Petersson

      Affiliations

    • Department of Cell and Molecular Biology, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden
    • ,
  • Richard Neutze

      Affiliations

    • Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, S-405 30 Göteborg, Sweden
    • Corresponding Author InformationCorresponding author. Fax: +46 31 786 3910.

Received 7 April 2010; accepted 14 April 2010. published online 21 April 2010.

Abstract 

Aquaporin-mediated water transport across cellular membranes is an ancient, ubiquitous mechanism within cell biology. This family of integral membrane proteins includes both water selective pores (aquaporins) and transport facilitators of other small molecules such as glycerol and urea (aquaglyceroporins). Eukaryotic aquaporins are frequently regulated post-translationally by gating, whereby the rate of flux through the channel is controlled, or by trafficking, whereby aquaporins are shuttled from intracellular storage sites to the plasma membrane. A number of high-resolution X-ray structures of eukaryotic aquaporins have recently been reported and the new structural insights into gating and trafficking that emerged from these studies are described. Basic structural themes reoccur, illustrating how the problem of regulation in diverse biological contexts builds upon a limited set of possible solutions.

Keywords: Aquaporin, Membrane protein structural biology, X-ray diffraction

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PII: S0014-5793(10)00321-2

doi:10.1016/j.febslet.2010.04.037

FEBS Letters
Volume 584, Issue 12 , Pages 2580-2588, 18 June 2010

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