Structure and Function of Membrane Proteins

Membrane proteins are mediators of essential processes in the cell such as solute transport, electrical excitability and signaling. Atomistic insight into the architecture of membrane proteins, their conformational breadth and precise functioning is essential in fundamental research. Since membrane proteins are major targets of small molecule drugs these insights are also necessary for the treatment of life-threatening diseases. In the Brunner lab we study the structure and function of membrane proteins, with a particular emphasis on lipid biology and ion channels in membrane transport.

Janine Brunner

Group Leader
Group Leader: VIB-VUB Center for Structural Biology, Brussels, Belgium
Postdoctoral Fellow: Paul Scherrer Institute, Laboratory of Biomolecular Research, Switzerland, 2018-2019
Postdoctoral Fellow: University of Basel, Biozentrum, Basel, Switzerland, 2017
Postdoctoral Fellow: University of Zürich, Department of Biochemistry, Zürich, Switzerland, 2016
PhD: University of Zürich, Department of Biochemistry, Zürich, Switzerland, 2015

Research areas

Structural biology

Research focus

Lipid transporters and membrane asymmetry
Our knowledge on the composition and architecture of biological membranes has grown substantially in the past decades. However, we are just beginning to functionally and structurally chara​​cterize the molecular identities that underlie the complex organization of bilayers.

One important feature of biomembranes is the asymmetric distribution of specific lipids between the two leaflets of the bilayer. This distribution is also subject to dynamic changes and serves important functions. For instance, exposure of phosphatidylserine to the extracellular leaflet– normally confined to the intracellular leaflet of the plasma membrane in the resting state – is a crucial event in processes as diverse as apoptosis, blood clotting, bone mineralization, myoblast fusion and in cell to cell spreading of viruses (apoptotic mimicry).

Read more

Crystal structure of the TMEM16 lipid scramblase from Nectria haematococca. The lipids traverse a hydrophilic membrane-facing spiral groove (arrows) in each subunit (yellow and cyan) upon activation by Ca2+.

Publications

To showcase the world-class scientific research of the Janine Brunner Lab, you can discover their scientific papers in more detail.

Jobs

We are always on the lookout for highly motivated colleagues to join our team. If you are interested, please contact us.

Team

The Janine Brunner Lab can only thrive thanks to the dedication and commitment of its people, no matter what their function or seniority.

Events 

To stay up to date in rapidly developing fields, scientists regularly interact with (international) colleagues. Conferences and other (scientific) events are an excellent way to facilitate such a continent-spanning knowledge exchange.