Pascal Meier

PhD student

Visa sidan på svenska
Works at Department of Biochemistry and Biophysics
Telephone 08-674 79 79
Visiting address Svante Arrhenius väg 16
Room A 557
Postal address Institutionen för biokemi och biofysik 106 91 Stockholm

About me

  • Travel Grant SGK/SSCr (Swiss Society for Crystallography), Switzerland - 2019
  • Travel Grant K & A Wallenberg Foundation, Sweden - 2019
  • Chairperson Central PhD Council (CDR) - 2020
  • Doktorandrepresentant member, University Board - 2020


Functional and structural study of Solute Carrier (SLC) Transporters
Research group: David Drew


A selection from Stockholm University publication database
  • Iven Winkelmann (et al.).
  • 2020. Iven Winkelmann (et al.). EMBO Journal 39 (24)

    Na+/H+ exchangers (NHEs) are ancient membrane-bound nanoma- chines that work to regulate intracellular pH, sodium levels and cell volume. NHE activities contribute to the control of the cell cycle, cell proliferation, cell migration and vesicle trafficking. NHE dysfunction has been linked to many diseases, and they are targets of pharma- ceutical drugs. Despite their fundamental importance to cell home- ostasis and human physiology, structural information for the mammalian NHEs was lacking. Here, we report the cryogenic elec- tron microscopy structure of NHE isoform 9 (SLC9A9) from Equus caballus at 3.2 Å resolution, an endosomal isoform highly expressed in the brain and associated with autism spectrum (ASD) and atten- tion deficit hyperactivity (ADHD) disorders. Despite low sequence identity, the NHE9 architecture and ion-binding site are remarkably most similar to distantly related bacterial Na+/H+ antiporters with 13 transmembrane segments. Collectively, we reveal the conserved architecture of the NHE ion-binding site, their elevator-like structural transitions, the functional implications of autism disease mutations and the role of phosphoinositide lipids to promote homodimerization that, together, have important physiological ramifications.

  • 2017. Abdul Aziz-Qureshi (et al.). A Structure-Function Toolbox for Membrane Transporter and Channels, 123-138

    Here, we present a simple overexpression condition for high-throughput screening of membrane proteins in Escherichia coli. For the vast majority of bacterial membrane protein targets tested the MEMbrane protein Single shoT Amplification Recipe-MemStarleads to high production yields of target protein. The use of MemStar has facilitated structural studies of several transport proteins.

Show all publications by Pascal Meier at Stockholm University

Last updated: March 19, 2021

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