Aquaporin Protein-Protein Interactions
Open Access
- 27 October 2017
- journal article
- review article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 18 (11), 2255
- https://doi.org/10.3390/ijms18112255
Abstract
Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner. Protein–protein interactions play crucial roles in both regulatory processes and also mediate alternative functions such as cell adhesion. In this review, we summarize recent knowledge about aquaporin protein–protein interactions; dividing the interactions into three types: (1) interactions between aquaporin tetramers; (2) interactions between aquaporin monomers within a tetramer (hetero-tetramerization); and (3) transient interactions with regulatory proteins. We particularly focus on the structural aspects of the interactions, discussing the small differences within a conserved overall fold that allow for aquaporins to be differentially regulated in an organism-, tissue- and trigger-specific manner. A deep knowledge about these differences is needed to fully understand aquaporin function and regulation in many physiological processes, and may enable design of compounds targeting specific aquaporins for treatment of human disease.Funding Information
- Swedish Research Council (2012-2849)
This publication has 139 references indexed in Scilit:
- Aquaporin 6 binds calmodulin in a calcium-dependent mannerBiochemical and Biophysical Research Communications, 2009
- Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass SpectrometryJournal of Proteome Research, 2009
- Evidence against Involvement of Aquaporin-4 in Cell–Cell AdhesionJournal of Molecular Biology, 2008
- Junction-forming aquaporinsCurrent Opinion in Structural Biology, 2008
- Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressinProceedings of the National Academy of Sciences of the United States of America, 2008
- FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localizationProceedings of the National Academy of Sciences of the United States of America, 2007
- Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channelProceedings of the National Academy of Sciences of the United States of America, 2006
- Pathogenesis and treatment of autosomal-dominant nephrogenic diabetes insipidus caused by an aquaporin 2 mutationProceedings of the National Academy of Sciences of the United States of America, 2006
- The channel architecture of aquaporin 0 at a 2.2-Å resolutionProceedings of the National Academy of Sciences of the United States of America, 2004
- T-coffee: a novel method for fast and accurate multiple sequence alignmentJournal of Molecular Biology, 2000