FEBS Letters Award Session
Sunday 31 August
14:00-14:30, Grand Auditorium
Lund University, SE Structural principles behind eukaryotic aquaporin regulation Since biological membranes only have limited water permeability they facilitate the transport of water in and out of the cell through membrane-bound water-specific protein channels known as aquaporins (AQP). The importance of this protein family is highlighted by the fact that the discovery of AQPs gave Peter Agre the Nobel Prize in Chemistry in 2003. Aquaporins can be found in all kingdoms of life ranging from bacteria to higher eukaryotes such as plants and humans and are highly conserved between species. Eukaryotic aquaporins are often regulated by mechanisms such as trafficking and/or gating, allowing for fine-tuning of the water transport across the membrane at different time points. For plants, this is crucial in order to adapt to water fluctuations in the environment. Dysfunctional regulation of aquaporins in humans have been shown to be involved in several disease states. We have solved the X-ray structures of the gated spinach aquaporin SoPIP2;1 as well as human AQP2 which is regulated by trafficking. These structures have not only allowed us to study the structure-function relationships of each individual aquaporin, but also, due to the high degree of sequence conservation within the aquaporin family, deepen our general understanding of aquaporin regulation and the structural principles behind this.Biography |
|||
|