Next Article in Journal
The Role of Gap Junction-Mediated Endothelial Cell–Cell Interaction in the Crosstalk between Inflammation and Blood Coagulation
Next Article in Special Issue
The Effect of Aquaporin 1-Inhibition on Vasculogenic Mimicry in Malignant Mesothelioma
Previous Article in Journal
The Peptidylarginine Deiminase Inhibitor Cl-Amidine Suppresses Inducible Nitric Oxide Synthase Expression in Dendritic Cells
Previous Article in Special Issue
A Review: Expression of Aquaporins in Otitis Media
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2017, 18(11), 2255; doi:10.3390/ijms18112255

Aquaporin Protein-Protein Interactions

Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 221 00 Lund, Sweden
*
Author to whom correspondence should be addressed.
Received: 17 September 2017 / Revised: 20 October 2017 / Accepted: 23 October 2017 / Published: 27 October 2017
(This article belongs to the Special Issue Aquaporins: Water Channels Essential for Living Organisms)
View Full-Text   |   Download PDF [9288 KB, uploaded 27 October 2017]   |  

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. View Full-Text
Keywords: aquaporin; protein-protein interactions; gating; trafficking; membrane channel; membrane protein aquaporin; protein-protein interactions; gating; trafficking; membrane channel; membrane protein
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Roche, J.V.; Törnroth-Horsefield, S. Aquaporin Protein-Protein Interactions. Int. J. Mol. Sci. 2017, 18, 2255.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top