Excited to share our work on the structure and function of cytoplasmic lattices within mouse embryos. A collaborative effort with @niakanlab.bsky.social and work led by @kashishsingh.bsky.social and @inaharasimov.bsky.social . It is now out on BioRxiv: www.biorxiv.org/content/10.6...

Excited to decode the intricate language of ubiquitin chains and unravel their role in protein degradation? 🧬🔬 👉 APPLY NOW to join the lab of Dr. Leo Kiss @leokiss.bsky.social @imprs-lm.bsky.social. #CellularBiochemistry #Ubiquitin #Proteostasis #ProteinDegradation

The E3 ubiquitin ligase mechanism specifying targeted microRNA degradation pubmed.ncbi.nlm.nih.gov/41851464/ #cryoem

Our work on the E3 ligase mechanism of target-directed microRNA degradation is now published! Amazing collaboration with Brenda Schulman’s lab led by @jakobfarnung.bsky.social and @elenaslo.bsky.social, with special thanks to @wyppeter.bsky.social, Lianne Blodgett, and Daniel Lin! tinyurl.com/Z8TDMD

Glückwunsch, Bruderherz! Really outstanding work by @bartellab.bsky.social and Schulman Lab. This is how transatlantic research is done 🇺🇸🇩🇪.

The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation (TDMD) is now published! 🎉🍾 We, @bartellab.bsky.social and Schulman lab, describe how 2-RNA factors control protein degradation by recruiting an E3 ligase. @mpibiochem.bsky.social www.nature.com/articles/s41...

Excited to announce that FASEB Ignite Career Forum 2026 (preceding FASEB Ubiquitin Mechanisms, Functions, and Therapeutics & Protein Folding in the Cell) is open for registration! Abstract deadline - April 6, 2026 For more details - events.faseb.org/event/Protei... events.faseb.org/event/Ubiqui...

Congratulations, @leokiss.bsky.social ! 🎉🎉 looking forward to the exciting research of the Kiss lab. This is a great opportunity for prospective PhD students interested in doing cutting-edge research 🧪 on ubiquitin!

🚨New preprint! We built a cell-free genomics platform (GATO-seq) to probe transcriptional regulation and discovered a “super pause” sequence that triggers a new Pol II active-site conformation. Huge shout-out to @robertovn.bsky.social for pulling off this monster of a project. tinyurl.com/superpause

🚨Preprint alert🚨 How does chromatin “architecture” form at CTCF sites? Our new preprint with @voslab.org and @andersshansen.bsky.social shows CTCF dimerization promotes nucleosome oligomerization on chromatin. tinyurl.com/CTCF-nucleos...

Happy to share part of my postdoctoral work at the @lucas.farnunglab.com lab. Great collaboration with @voslab.org and @andersshansen.bsky.social. “Structural basis for CTCF-mediated chromatin organization” www.biorxiv.org/content/10.6...

🧪🧬New preprint We present cryo-EM structures of reconstituted CTCF–nucleosome complexes, showing CTCF dimerization drives nucleosome oligomerization into defined higher-order assemblies. Disrupting CTCF–CTCF interfaces in mESCs reduces looping and impairs differentiation. tinyurl.com/CTCF-nucleos...

Formation & function of #MembranelessOrganelles! #CryoET structures of #proteasome storage granules inside cells! Read our paper @cp-cell.bsky.social! ❕Publication: doi.org/10.1016/j.ce... ❕Press Release: www.biochem.mpg.de/en/pressroom @uoftmedicine.bsky.social @erc.europa.eu #UPSmeetMet

We’re excited to share our latest preprint on the mechanism of excised linear intron stabilization in yeast! This work was led by PhD student @glennli.bsky.social and was a wonderful collaboration with @maxewilkinson.bsky.social. Link: www.biorxiv.org/content/10.6... (1/4)

Pour a glass of champagne AND red Bordeaux—Our newest work with GSK @scripps.edu is out in @nature.com! Here we describe SB-405483, the first allosteric CRBN ligand which potentiates neosubstrate degradation. Congrats Vanessa and all authors! 🍷💫💐 www.nature.com/articles/s41...

This is also a good occasion to highlight that we are looking for post-doctoral researchers that are interested in understanding the fundamental mechanisms of transcription, DNA replication, and chromatin.

Check out the newest preprint from the Schulman lab 🎊🎉 Super cool mechanism of how a metabolite regulates the stability of its own metabolizing enzyme! Alina did it all for this project CRISPR screen ✂️, biochemistry 🧪, and cryo-EM ❄️🔬. Congrats!

What happens when E3 Ubiquitin Ligase and RNA Enthusiasts team up! Massive congrats to this transatlantic collaboration between @jakobfarnung.bsky.social from Schulman Lab and @elenaslo.bsky.social from @bartellab.bsky.social Have a read!

The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation www.biorxiv.org/content/10.64898/2026.01.05.697729v1 #cryoem

Look at this super exciting E3, recognizing the specific RNA-bound state of it’s target protein alone! Massive Congrats @jakobfarnung.bsky.social and collaborators from @bartellab.bsky.social

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).

New research group leader @matthiasmuhar.bsky.social joins @mpi-cbg.de! 🥳 With his group "Functional genomics of proteome remodeling,” Matthias wants to pursue high-throughput genetic studies to understand how protein turnover is regulated. Welcome, Matthias! www.mpi-cbg.de/news-outreac...

Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1 https://www.biorxiv.org/content/10.1101/2025.11.14.688510v1

Check out the latest work from our lab, led by Daniel Lin and Lara Elcavage: www.biorxiv.org/content/10.1... (1/3)

Have a look at this Tools of the Trade Article I wrote for @natrevmcb.nature.com on decoding #ubiquitin signals inside cells using UbiREAD! Many thanks to @lisaheinke.bsky.social for the opportunity to write this TotT!

ICYMI: New Online! Decoding ubiquitin signals inside cells

🧬 Transcription elongation by RNA polymerase II relies on a web of elongation factors. Our new work shows how IWS1 acts as a modular scaffold to stabilize & stimulate elongation. Fantastic work by Della Syau! www.biorxiv.org/content/10.1...

Excited to share our latest study in @natcomms.nature.com , where we characterize the chaperone function of the ER membrane protein complex (EMC)—supporting membrane protein biogenesis beyond insertion! 1/9 www.nature.com/articles/s41...

Excited about #ubiquitin and #TPD ? Then join us tomorrow for the latest instalment of the @danafarber.bsky.social ‬ Targeted Protein Degradation Webinar where Kimberly Stegmaier and I will present our latest work. dfci.zoom.us/webinar/regi...

Congratulations to our own Lucas Farnung @lucas.farnunglab.com who has been named as one of 30 Freeman Hrabowski Scholars for 2025 by the Howard Hughes Medical Institute (HHMI). So well deserved deserved !! www.hhmi.org/programs/fre...

Schulman lab is ready for the GRK2243 Symposium: Understanding ubiquitination: from molecular mechanisms to disease in würzburg #wUeBI2025 @grk2243.bsky.social @jakobfarnung.bsky.social @samuelmaiwald.bsky.social @hannahbkmpr.bsky.social

Super cool story on branched UB chain formation. Congrats Sam!

Excited to share our latest study on how K29/K48-branched #ubiquitin chains are forged by the #E3 ligase TRIP12, and how this suggests a consensus mechanism for chain formation by HECT E3s! @natsmb.nature.com 1/7 www.nature.com/articles/s41...

 🧬🎉Thrilled to share our new chromatin remodeling study! We reveal three states of human CHD1 and identify a novel "anchor element" that interacts with the acidic patch—conserved among remodelers. Our structures clarify mechanisms of remodeler recruitment! Link: authors.elsevier.com/a/1l2ik3vVUP...

New Preprint: We have solved the structure of the proteasome in complex with two different ubiquitin chains: www.biorxiv.org/content/10.1... This work is spearheaded by PhD Student Sascha Amann Let me walk you through it 🧵 1/9

If you are interested in Ubiquitin this paper is a must read! Congrats Leo!

It's finally out – actually out and in print! Many thanks to @jcornlab.bsky.social @matthiasmuhar.bsky.social @jakobfarnung.bsky.social and all the fantastic collaborators. What started as pure curiosity lead to an amazing find! www.nature.com/articles/s41...

Today in @nature.com we share our back-to-back stories with Ning Zheng’s lab revealing chemical-genetic convergence between a molecular glue degrader & E3 ligase cancer mutations. 1/5

Excited about mechanistic biology and processes in the cell's nucleus? Join our lab as a post-doctoral researcher! We have a state-of-the-art cryo-EM facility (new microscopes coming!), a brand-new lab space, and a vibrant community at HMS! DM/email me or check farnunglab.com for more info.

Our story on the mechanism of co-transcriptional histone mark deposition is now officially out: www.science.org/doi/10.1126/...

Cells are filled with toxic stuff that damages healthy proteins. Is that garbage just left to rot on the curb? No way! Ubiquitin ligases have evolved to recognize chemical damage and clean it up! www.nature.com/articles/s41...

scary but fascinating - cells have a degradation pathway that hunts down C-terminal scars (amides!) on damaged proteins. just wow. chemical biology plus CRISPR at its best. big congrats to all authors! www.nature.com/articles/s41...

Very excited to highlight @jcornlab's beautiful work on the E3 ligase SCF-FBXO31, which recognizes chemically damaged proteins. Mutations in FBXO31 cause disease by substrate-rewiring, really cool. Congratulations to all authors! rdcu.be/d7WGc

Super exiting new work revealing a novel quality control pathway for c-terminal amides!

On the degradation of damaged cellular proteins via C-terminal amidation. By Alfred Freeberg & @micharapelab.bsky.social. @ispt-proteinterm.bsky.social www.nature.com/articles/d41...

🎉Super excited to share our story on how the substrate receptor FBXO31 functions as a quality control factor by recognizing amides. This has been an amazing collaboration between Bode lab and @jcornlab.bsky.social. Special shutout goes to @matthiasmuhar.bsky.social www.nature.com/articles/s41...

Our paper describing a novel DNA binding mode for MORC2 is published! Congratulations to Nika Fendler on her first, first author paper. This was an epic effort and revealed many new and unpredicted functions for MORC2. You can read about it here: tinyurl.com/MORC2-DNA

🎄 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...

Ever wondered how transcription choreographs histone modifications? Our work reveals the basis of co-transcriptional H3K36me3 by SETD2. We visualize how a histone writer coordinates with the transcription machinery! This is the magnus opus of @jonmarkert.bsky.social! tinyurl.com/setd2

Our Synthesis Tag (SynTag) for the synthesis of aggregating peptides and proteins is now published in JACS 🥳 Congratulations to first authors Héloïse & Elyse and everyone else involved ✨✨ pubs.acs.org/doi/10.1021/...