Dan Grabarczyk

Registration now open for #EMBOUbiquitin.
meetings.embo.org/event/26-ubi...

Childcare, accessibility, and travel grants available.

#ubiquitin #TargetedProteinDegradation #Proteostasis #UBL

We are excited to be recruiting a new tenure track group leader in the Structural Studies Division at MRC LMB! It is an amazing place to start your own lab.
@mrclmb.bsky.social

Please get in touch if you have any questions.
www.nature.com/naturecareer...

ChimeraX screenshot showing CubeNTube plugin.

The new ChimeraX CubeNTube plugin allows erasing parts of maps using cube, cylinder, and custom shapes and has undo. Created by Tamino Cairoli. Available from ChimeraX menu Tools / More Tools....

Our paper is out in @natcomms.nature.com! APOBEC3s drive mutagenesis in cancer. We uncover a novel pathway keeping them in check. The key is APOBEC3 binding of cellular RNAs, which simultaneously controls their nuclear localization and shields them from degradation.

Read it here: rdcu.be/e4qaa

To regulate gene activity, proteasomes - waste disposal machines of cells - must enter the nucleus. IMP Researchers now show how the adaptor protein AKIRIN2 helps ferry this massive complex through the nuclear pore: https://www.nature.com/articles/s41467-026-69162-0

Some cool E3 ligase structures here with calmodulin-mediated oligomerisation. Also interesting collection/processing to deal with preferred orientation.

www.biorxiv.org/content/10.6...

@lorenzoorts.bsky.social previously worked as a postdoctoral fellow at @impvienna.bsky.social in Austria. She will establish a new lab at IMB to investigate how mRNA translation is activated in the early embryo. Welcome to IMB Laura! 💐

Read more here: www.imb.de/about-imb/ne...

After a long (but fun!) postdoc journey, I am very excited to share that I will start my own lab in the Ubiquitin Signalling Division at WEHI. We will study how ubiquitin controls mitochondrial health and its role in neurodegenerative disease. Hiring soon!

When RNA Degradation 🤝 meets 🤝 Protein Degradation! tinyurl.com/E3TDMD In a collaboration of @bartellab.bsky.social and Schulman lab, we show that, in target-directed microRNA degradation (TDMD), 2-RNA-factors recruit an E3 ligase and induce the degradation of not only a protein but also RNA (1/5).

The vault associates with membranes in situ The eukaryotic vault particle is a giant ribonucleoprotein complex that assembles into an iconic barrel-like cage. Its cellular function has remained elusive despite extensive characterization. Using ...

Vaults. They are cell biology's greatest puzzle! This preprint from Martin Beck's lab shows them docked on ER membranes with a ribosome inside. What on earth is going on there??

#CellBiology #WTFology

www.biorxiv.org/content/10.6...

🤯

SAVE THE DATE!
The EMBO workshop "Ubiquitin and Ubiquitin-like proteins in Health and Disease" will be on September 2026.
Exciting line up of talks and an amazing location!
Organised by @kulathu.bsky.social, @merbllab.bsky.social, @simonapolo.bsky.social, Claudio Joazeiro.
Registration open soon.

Filament formation and NAD processing by noncanonical human FAM118 sirtuins Nature Structural & Molecular Biology - Baretić and Missoury et al. identify vertebrate proteins FAM118B and FAM118A as sirtuins similar to bacterial antiphage enzymes and show that...

Very happy to share our collaborative project on FAM118 proteins - noncanonical sirtuins that form filaments and process NAD in human and other vertebrate cells.

Degrons and degradation signals beyond short linear motifs - Nature Chemical Biology Degrons are degradation signals in target proteins to direct recognition and degradation by the ubiquitin–proteasome system. Wang et al. introduce degrons of different types, with an emphasis on high-...

A new Review discusses how degrons of different types, with an emphasis on high-order structural ones, regulate substrate-E3 interactions and how their dysregulation is linked to human diseases

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

An Asgard archaeon with internal membrane compartments

Brilliant study led by @fmacleod.bsky.social and Andriko von Kügelgen. Tight collaboration with @buzzbaum.bsky.social and lab. Congrats to all authors!

www.biorxiv.org/content/10.1...

📢 Open Call! The Max Perutz Labs invite applications for a Full Professorship in Integrative Structure Biology with a focus on in situ structural biology using cryo-electron tomography (cryo-ET) and related methods. More details ➡️ tinyurl.com/brswbymu

Split-site ubiquitination gives ZNFX1 new power in RNA defense Recent work by Grabarczyk et al. uncovers the molecular mechanism by which ZNFX1, an interferon-stimulated gene, employs a novel split-site E3 ligase domain structure to ubiquitinate both protein lysi...

Split-site ubiquitination gives ZNFX1 new power in RNA defense @cellcellpress.bsky.social
www.cell.com/molecular-ce...
www.sciencedirect.com/science/arti...

Elaborate machinery for inserting proteins into the outer membrane of bacteria Bacteria in the gut use an unusual molecular apparatus to insert complex proteins into their outer membrane.

Elaborate machinery for inserting proteins into the outer membrane of bacteria www.nature.com/articles/d41...

Structure and substrate recognition by the Twin-arginine translocation (Tat) pathway core complex https://www.biorxiv.org/content/10.1101/2025.09.18.677151v1

Dimerization for activation - Nature Chemical Biology Nature Chemical Biology - Dimerization for activation

Thanks a lot to Yiyun Song @natchembio.nature.com for highlighting our ZNFX1 paper. www.nature.com/articles/s41...

We have an open post-doc position in my group to study mRNA cleavage and polyadenylation using biochemical reconstitution and cryoEM.

Please get in touch if you are interested in joining this amazing team! 🔬🧬🤩
#RNA #cryoEM

I am excited to share our new preprint on the CAGE complex, a mysterious hollow protein complex that I first saw years ago while surveying Tetrahymena ciliary lysate www.biorxiv.org/content/10.1... #cilia #protistsonsky 🧬🧪

I am excited to announce that I will be moving to IMB Mainz next year! The Winter call for the IPP PhD program is now open; if you are interested in maternal #mRNA regulation and #translation in early vertebrate development, please apply! Deadline: 16 October.

More info: www.imb.de/students-pos...

ZNFX1 uses two-component ubiquitin circuitry to quarantine viral RNA The detection of viral RNA inside cells triggers a diverse range of antiviral responses, including global translation inhibition, interferon secretion and RNA sequestration. Mutations in the gene ZNFX...

Pre-print: our description of RZ affiliate ZNFX1 is now online.

On binding viral RNA, ZNFX1 generates parallel Ub currents, coordinating Ub-dependent RNA silencing and aggregate resolution.

Huge effort from first authors Dan Squair and @eilidhrivers.bsky.social

www.biorxiv.org/content/10.1...

Inside the cell’s recycling hub: unveiling the architecture of UBR4 Researchers from the lab of Tim Clausen and collaborators have unveiled the three-dimensional structure of UBR4, a giant protein complex that safeguards cells by targeting defective proteins for destr...

Researchers around @clausenlab.bsky.social & @dangrabarczyk.bsky.social have unveiled the three-dimensional structure of UBR4, a giant protein complex that safeguards cells by targeting defective proteins for destruction—offering fresh insights into health & disease. www.science.org/doi/10.1126/...

We had great help from Hyun Kyu Song's lab who got crystal structures of substrate complexes, as well as our ongoing collaboration with the Manu Hegde lab. Also thanks to the efficient review process which really pushed us to improve the paper.

Glad to share the final version of our story about the UBR4 complex, an E4 ligase protein quality control hub @science.org. Now with more cryo-EM structures and a deeper dive into substrate recognition, especially escaped mitochondrial proteins @clausenlab.bsky.social www.science.org/doi/10.1126/...

ZNFX1 compacts and tags RNA to keep immunity in check Tim Clausen’s lab at the IMP and collaborators have uncovered how the ancient immune protein ZNFX1 enables cells to walk the fine line between fighting infection and avoiding autoimmune damage. The te...

Scientists uncovered how the immune protein ZNFX1 enables cells to walk the fine line between fighting infection & avoiding autoimmune damage. ZNFX1 can ubiquitinate & compact host & viral RNA into molecular condensates, extending ubiquitin biology to RNA itself. More: www.imp.ac.at/news/article...

A split-site E3 ligase mechanism enables ZNFX1 to ubiquitinate and cluster single-stranded RNA into ubiquitin-coated nucleoprotein particles Grabarczyk et al. show the structure and mechanism of a non-canonical ubiquitin ligase, which is activated through nucleic-acid-induced oligomerization and is critical for cell survival during immune ...

Happy to share our work on the structure and function of the unusual E3 ligase ZNFX1 @cp-cell.bsky.social. It uses a nucleic acid-activated transthiolation mechanism, ubiquitinating and clustering RNA to protect cells in an immune response. @clausenlab.bsky.social
www.cell.com/cell/fulltex...

Opening for a biochemist to help us in the characterisation of novel ubiquitin-based antivirals. Diverse backgrounds welcomed; a keen sense of adventure is a must 😁

Details and criteria are below; please get in touch with any questions.

www.jobs.gla.ac.uk/job/research...