Aquaporin Protein-Protein Interactions
AbstractAquaporins 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. View Full-Text
Share & Cite This Article
Roche, J.V.; Törnroth-Horsefield, S. Aquaporin Protein-Protein Interactions. Int. J. Mol. Sci. 2017, 18, 2255.
Roche JV, Törnroth-Horsefield S. Aquaporin Protein-Protein Interactions. International Journal of Molecular Sciences. 2017; 18(11):2255.Chicago/Turabian Style
Roche, Jennifer V.; Törnroth-Horsefield, Susanna. 2017. "Aquaporin Protein-Protein Interactions." Int. J. Mol. Sci. 18, no. 11: 2255.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.