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Dutzler lab

@dutzlerlab.bsky.social
42 followers 30 following 3 posts

Membrane protein enthusiasts at the University of Zurich.

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Reposted by Dutzler lab
Nature Communications @natcomms.nature.com · 22/09/2026
Researchers from @dutzlerlab.bsky.social define the role of the intracellular sub-domain (ISD) of the obligatory LRRC8A subunit in LRRC8 channel activation
dlvr.it
The intracellular subdomain of the volume-regulated anion channel subunit LRRC8A is a hotspot of channel activation - Nature Communications
Ion channels of the LRRC8 family are modular proteins consisting of a transmembrane pore and cytoplasmic regulatory domains. Here the authors combine structural and functional data to define the role of the intracellular sub-domain (ISD) of the obligatory LRRC8A subunit for channel activation.
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Reposted by Dutzler lab
Nature Communications @natcomms.nature.com · 22/09/2026
Authors from @dutzlerlab.bsky.social describe the architecture of channels assembled from LRRC8A and D subunits, and their conformational changes during activation
dlvr.it
Structures of the volume-regulated anion channel LRRC8A/D in activating and inhibiting conditions - Nature Communications
Members of the LRRC8 family form heteromeric ion channels that are activated upon cell swelling. Here authors describe the architecture of assemblies of LRRC8A and D subunits and their conformational changes during activation.
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Reposted by Dutzler lab
Nature Methods @natmethods.nature.com · 29/08/2025
A laser flash melting procedure, followed by rapid revitrification, provides a simple approach to help mitigate the preferred orientation problem that plagues cryo-EM analysis. www.nature.com/articles/s41...
nature.com
Laser flash melting cryo-EM samples to overcome preferred orientation - Nature Methods
Individual proteins tend to adopt preferred orientations when subjected to vitrification for cryo-electron microscopy analysis. A laser flash melting procedure followed by rapid revitrification provid...
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Reposted by Dutzler lab
melaniearndt.bsky.social @melaniearndt.bsky.social · 28/08/2025
The second part of my PhD work is now out in NSMB! 🚨✨ We explored how IST2, a known ER–plasma membrane tether in S. cerevisiae, facilitates lipid transfer at membrane contact sites. Check it out: www.nature.com/articles/s41...
nature.com
Structural basis for lipid transport at membrane contact sites by the IST2–OSH6 complex - Nature Structural & Molecular Biology
IST2 serves as a tether between the endoplasmic reticulum and the plasma membrane in yeast. Here, Arndt et al. interrogate its interaction with OSH6, revealing that the two proteins remain associated ...
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Dutzler lab @dutzlerlab.bsky.social · 15/07/2025
Check out the recent Alzforum article about our lab’s paper on TTYH2 and ApoE! www.alzforum.org/news/researc...
alzforum.org
ApoE and Tweety Homolog 2—Proteins that Flock Together? | ALZFORUM
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Dutzler lab @dutzlerlab.bsky.social · 27/06/2025
🚨 Anastasiia’s latest paper is out! We discovered that TTYH2 and ApoE bind in the endosomal lumen, where TTYH2 then facilitates lipid transfer from ApoE into the endosomal membrane. Check it out now in Nature: www.nature.com/articles/s41...
nature.com
Interactions between TTYH2 and APOE facilitate endosomal lipid transfer - Nature
The Tweety homologue TTYH2 is identified as the lipid transfer mediator for APOE-containing lipoproteins.
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