Dan Grabarczyk

New preprint: In situ Architecture of #Plasmodesmata.

Using #cryoET, #AlphaFold & proteomics, we uncover the native organization of plant intercellular nanopores.

🔗 doi.org/10.1101/2025...

🧪🧵1/n
#teamtomo #PlantScience #Physcomitrium #Arabidopsis #cryoEM

26.07.2025 15:38 — 👍 189    🔁 71    💬 9    📌 8

🎉 Congratulations to our Daniel Grabarczyk, research associate in the Clausen lab, who has been awarded a prestigious FWF Principal Investigator Project Grant to support his research into the molecular mechanisms of innate immunity against viruses.

Read more: www.imp.ac.at/news/article...

09.07.2025 08:53 — 👍 25    🔁 3    💬 2    📌 0

In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex Cryo-electron tomography has emerged as powerful technology for in-cell structural biology, and in combination with breakthroughs in protein structure prediction, offers a unique opportunity for illum...

This is just an excellent preprint by Rasmus Jensen and colleagues from Julia Mahamid's lab @embl.org - a tour de force of Cryogenic electron tomography to do in cell structural biology in which they discover a new complex and solve its structure and function! www.biorxiv.org/content/10.1...

22.05.2025 19:00 — 👍 44    🔁 19    💬 2    📌 1

ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213 - Nature Communications RNF213 is an E3 ligase with ATPase activity. Here, the authors show that RNF213 is activated by ATP binding and senses cellular energy states, and reveal a transthiolation mechanism induced by immune ...

Great to see this out. A story that spanned continents, cities and budget codes…

www.nature.com/articles/s41...

Big thanks to all the teams involved!

@clausenlab.bsky.social @e3chembio.bsky.social

13.05.2025 09:51 — 👍 54    🔁 28    💬 3    📌 1

Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination - Nature Communications The K29/K48 hetero-polyubiquitin signal has been reported to be an enhanced degradation signal, but the enzymatic mechanism of this ubiquitin chain formation is unclear. Here, the authors reveal how t...

Amazing chemical biology/structural biology work on K29/K48 branching E3 Ufd4/TRIP12 www.nature.com/articles/s41...

10.05.2025 12:05 — 👍 10    🔁 5    💬 0    📌 0

Thrilled to share the structure of dimerised human PINK1 docked to an endogenous translocase array on the mitochondrial surface, composed of two TOM complexes, bridged by a VDAC2 dimer! Published today in Science www.science.org/doi/10.1126/...

@wehi-research.bsky.social @komanderlab.bsky.social

13.03.2025 19:19 — 👍 167    🔁 57    💬 9    📌 6

Architecture of the 1.3 MDa complex of human UBR4 (2 x UBR4/KCMF1/CALM1). Picture shows top and side views of the cryo-EM density map and the modeled structure, colored by protein components and domains.

🎄 xmas preprint 🎄 we are excited to share our cryo-EM structure of UBR4 in complex with KCMF1 and CALM1. the PQC ligase forms a massive ubiquitination arena, primed to amplify ubiquitin chains (E4 activity) and boost degradation of defective proteins. www.biorxiv.org/content/10.1...

21.12.2024 10:46 — 👍 132    🔁 37    💬 3    📌 4

Happy to share our UBR4 structures. Check out the preprint to see how this giant E4 ligase complex selects substrates for ubiquitin chain extension. We also look at conservation and adaptations across humans, nematodes and plants.
www.biorxiv.org/content/10.1...
@clausenlab.bsky.social

21.12.2024 09:13 — 👍 66    🔁 16    💬 2    📌 1

SAVE THE DATE 🗓️Ubiquitin & Friends Symposium: 8-9 May 2025 in Vienna!
Registration will open🔜 Keep an eye out for the announcement 👀
✨guest speaker lineup👇🧵 +talks from abstracts! Great chance for #ECRs to meet with peers & experts in a friendly setting!
🔗 www.protein-degradation.org/symposium/

29.11.2024 14:18 — 👍 60    🔁 28    💬 1    📌 4