Seminar: Dr. S. Törnroth-Horsefield

Structural basis for regulation of eukaryotic aquaporins

Date:
16 October 2013 00:00 hrs.
Location:
Figdor Lecture Theatre, 8th floor RIMLS Building, Geert Grooteplein 26-28, route 289
Title:
Structural basis for regulation of eukaryotic aquaporins
Speaker(s):

Dr. Susanna Törnroth-Horsefield, Department of Biochemistry and Structural Biology, Lund University, Sweden

 

Host(s):

Prof. Peter Deen, Department of Physiology, RUMC

16-10-2013 00:00:00Europe/AmsterdamStructural basis for regulation of eukaryotic aquaporins Figdor Lecture Theatre, 8th floor RIMLS Building, Geert Grooteplein 26-28, route 289Rimlsrimls@radboudumc.nl

Remarks / more information:

Tornroth -HorsefieldSince 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 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. In humans, aquaporins have been implicated in cancer, brain oedema, cardiac and vascular complications, diabetes insipidus and many other disease states.

We have solved the X-ray structures of three eukaryotic aquaporins; the gated spinach aquaporin SoPIP2;1 as well as the structures of human AQP2 and AQP5,  both of which are 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.

Seminar 16-10-2013 Figuur

Fig. X-ray structures of SoPIP2;1 (left), human AQP2 (middle) and human AQP5 (right)

Selected publications:

  • Frick A, Järvå M, Törnroth-Horsefield S.FEBS Lett. 2013 Apr 2;587(7):989-93   Structural basis for pH gating of plant aquaporins. 
  • Horsefield R, Nordén K, Fellert M, Backmark A, Törnroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, Neutze R.Proc Natl Acad SciUSA. 2008 Sep 9;105(36):13327-32. High-resolution x-ray structure of human aquaporin 5.                                               
  • Törnroth-Horsefield S, Wang Y, Hedfalk K, Johanson U, Karlsson M, Tajkhorshid E, Neutze R, Kjellbom P.Nature. 2006 Feb 9;439(7077):688-694. Structural mechanism of plant aquaporin gating.
  • Yankovskaya V#, Horsefield R, Törnroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S.Science.2003 Jan 31;299(5607):700-704. Architecture of succinate dehydrogenase and reactive oxygen species generation.
  • Jormakka M, Törnroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.Science.2002 Mar 8;295(5561):1863-1868

 



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