VIB-VUB Center for Structural Biology Brunner Lab

Home

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.

VIB-200.jpeg

Janine Brunner

Since 2020      VIB group leader at VIB-VUB Center for Structural Biology in Brussels, Belgium

2018 - 2019     Postdoc, Paul Scherrer Institute (ETH), Switzerland

2017                 Postdoc, Biozentrum (University of Basel), Switzerland

2015 - 2016     Postdoc, University of Zürich, Switzerland

2010 - 2015     PhD, University of Zürich, Switzerland

Contact Janine on LinkedIn X Bluesky ORCID Google scholar

Selected publications

Stereoselectivity and functional plasticity of a common ligand-binding pocket in TRPM3. Bazeli B, Shkumatov AV, Schenck S, Vanherck J, Janssens A, Spieser SAH, Marchand D, Roelens R, Chaltin P, Marchand A, Vriens J, Voets T@, Brunner JD@. Nature Communications. 2026 Apr 1. doi: 10.1038/s41467-026-71226-0. Epub ahead of print. PMID: 41922314.

MISO: Microfluidic protein isolation enables single particle cryo-EM structure determination from a single cell colony. Gangadhar Eluru, Steven De Gieter, Stephan Schenck, Annelore Stroobants, Binesh Shrestha, Paul Erbel, Janine D. Brunner, Rouslan G. Efremov@. Nature Methods. 2025 Dec;22(12):2563-2573. doi: 10.1038/s41592-025-02894-x. Epub 2025 Nov 13. PMID: 41233542.

Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams. Schenck S, Laeremans T, Steyaert J, Brunner JD@. Nature Communications. 2025 May 5;16(1):4172. doi: 10.1038/s41467-025-59545-0. PMID: 40325068; PMCID: PMC12053756.

Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation. Mathieu Botte, Dongchun Ni, Stephan Schenck, Iwan Zimmermann, Mohamed Chami, Nicolas Bocquet, Pascal Egloff, Denis Bucher, Matilde Trabuco, Robert K. Y. Cheng, Janine D. Brunner, Markus A. Seeger, Henning Stahlberg & Michael Hennig@. Nature Communications 13, 1826 (2022). 

Structural basis for ion selectivity in TMEM175 K+ channels. Brunner JD@, Jakob RP, Schulze T, Neldner Y, Moroni A, Thiel G, Maier T, Schenck S@. Elife. 2020 Apr 8;9:e53683. doi: 10.7554/eLife.53683. PMID: 32267231; PMCID: PMC7176437. 

X-ray structure of a calcium-activated TMEM16 lipid scramblase. Brunner JD, Lim NK, Schenck S, Duerst A, Dutzler R@. Nature. 2014 Dec 11;516(7530):207-12. doi: 10.1038/nature13984. Epub 2014 Nov 12. PMID: 25383531.