Melanie Arndt

ORCID: 0000-0001-5000-3021
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About
Contact & Profiles
Research Areas
  • Ion channel regulation and function
  • Force Microscopy Techniques and Applications
  • Signaling Pathways in Disease
  • Mass Spectrometry Techniques and Applications
  • Ion Transport and Channel Regulation
  • Chemistry and Stereochemistry Studies
  • Advanced Electron Microscopy Techniques and Applications

University of Zurich
2022-2024

Membrane contact sites (MCS) are hubs for inter-organellar lipid transport within eukaryotic cells. As one of the principal tethers bridging ER and plasma membrane in Saccharomyces cerevisiae, protein Ist2 plays a major role during between both compartments. Here, we present comprehensive investigation elucidating structural mechanistic properties its interaction with soluble Osh6. The ER-embedded transmembrane domain is homologous to TMEM16 family acts as constitutively active scramblase....

10.1101/2025.02.18.638816 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2025-02-21

Abstract TMEM16F, a member of the conserved TMEM16 family, plays central role in initiation blood coagulation and fusion trophoblasts. The protein mediates passive ion lipid transport response to an increase intracellular Ca 2+ . However, mechanism how facilitates both processes has remained elusive. Here we investigate basis for TMEM16F activation. In screen residues lining proposed site conduction, identify mutants with strongly activating phenotype. Structures these determined herein by...

10.1038/s41467-022-34497-x article EN cc-by Nature Communications 2022-11-05

Abstract Transmembrane protein 16 F (TMEM16F) is a Ca 2+ -activated homodimer which functions as an ion channel and phospholipid scramblase. Despite the availability of several TMEM16F cryogenic electron microscopy (cryo-EM) structures, mechanism activation substrate translocation remains controversial, possibly due to restrictions in accessible conformational space. In this study, we use atomic force under physiological conditions reveal range structurally mechanically diverse assemblies,...

10.1038/s41467-023-44377-7 article EN cc-by Nature Communications 2024-01-02
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