Excited to share our latest work on understanding CTLH-MKLN1 substrate recruitment. Stay tuned for the paper 🤗

bioRxiv Biochemistry@biorxiv-biochem.bsky.social · 2w ago

Multimodal substrate recruitment enables CTLH-MKLN1 E3 ligase to target N-, C-, and internal degrons https://www.biorxiv.org/content/10.64898/2026.09.10.750665v1

Multimodal substrate recruitment enables CTLH-MKLN1 E3 ligase to target N-, C-, and internal degrons https://www.biorxiv.org/content/10.64898/2026.09.10.750665v1

⚡Preprint alert⚡ So proud of @amohamed98.bsky.social! Abdallah determined the cryo-EM structure of BRD4 bound to the kinase P-TEFb, defining the molecular basis of this key transcription interaction — and revealing that BRD4 and AFF4 binding are mutually exclusive to P-TEFb. Lots more inside 👇

Abdallah Mohamed@amohamed98.bsky.social · 3w ago

New preprint: in the last bit of my graduate work in the @voslab.org, we describe the mechanism for how BRD4 engages with P-TEFb in the context of regulating early RNA Pol II elongation. Read more here: www.biorxiv.org/content/10.6...

Very happy to see the final version of our work on the structure and composition of cytoplasmic lattices in mouse embryos, previously shared on bioRxiv, now published in The EMBO Journal! Many thanks to our editor, Ieva Gailite, and the reviewers for their constructive input.

The EMBO Journal@embojournal.org · 2mo ago

What’s the function of embryonic ‘cytoplasmic lattices’? Using cryo-ET, @kashishsingh.bsky.social @carter-lab.bsky.social and coworkers reveal them as megadalton-size hubs of ubiquitination proteins/ubiquitin transfer link.springer.com/article/10.1...

Extremely happy to see that my latest work on understanding how ARISC-RAP80 recognises and cleaves ubiquitin chains is now published @natcomms.nature.com Check it out if you are interested in #DUBs, #DNA repair, or #cryo-EM: www.nature.com/articles/s41...

Mechanism of K63-linked polyubiquitin recognition and cleavage by the BRCA1-A complex - Nature Communications

How the BRCA1-A complex finds and removes ubiquitin signals at DNA breaks remains unknown. Here the authors show that ARISC–RAP80 binds K63-linked ubiquitin chains through multiple subunits and non-ca...

nature.com

link.springer.com/article/10.1...

In-situ cryo-ET of mouse embryos reveals cytoplasmic lattices contain ubiquitin-charged E2-E3 ligase assemblies - The EMBO Journal

Cytoplasmic lattices (CPLs) are filamentous assemblies essential for mammalian embryonic development. They are known to regulate organelle organization, spindle assembly, and protein homeostasis, but ...

link.springer.com

⚡New preprint from the lab⚡: A key early checkpoint in gene expression is promoter proximal pausing of RNA polymerase II. For over 20 years, we as field have not been able to recreate pausing under realistic cellular conditions. @robertovn.bsky.social shows that ELOF1 is the missing piece.

Roberto Vázquez Núñez@robertovn.bsky.social · 4mo ago

🚨 New preprint: GATO-seq did it again! ELOF1 is the missing promoter-proximal factor that confers RNA Pol II resistance to TFIIF. Including ELOF1, DSIF, and NELF in GATO-seq reactions recapitulates promoter-proximal pausing in vitro at physiological conditions for the 1st time. tinyurl.com/ELOF1

Excited that Della Syau's PhD work is now available as a NAR Breakthrough article: academic.oup.com/nar/article/.... Della's work clarifies how IWS1 engages the transcription elongation complex, stimulates transcription, and controls association of other factors such as RECQL5.

Structure and function of IWS1 in transcription elongation

Abstract. Transcription elongation by RNA polymerase II is a tightly regulated process that requires coordinated interactions between transcription elongat

academic.oup.com

New work from the Schulman Dept. shows mechanisms of metabolite-regulated E3 ligase activity. Read more about it: “Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1” in Nature Communications. www.nature.com/articles/s41...

The Farnung Lab is looking for postdoctoral researchers interested in understanding mechanisms at the intersection of chromatin, transcription, and replication. Find out more here: www.farnunglab.com

Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1 pubmed.ncbi.nlm.nih.gov/42098103/ #cryoEM

BenchOS.ai just received an update. Check out the feature section to see what you ca do with BenchOS.

Thrilled to see this work published. Thanks to helpful reviewer suggestions, there are some exciting new insights that were not in the preprint (particularly in Figure 4). www.nature.com/articles/s41...

MRC Laboratory of Molecular Biology@mrclmb.ac.uk · 5mo ago

The hidden rules behind mRNA transport. A collaborative study between @simonbullock11.bsky.social & @carter-lab.bsky.social’s groups has found a structural code that explains how cells selectively transport mRNAs. Read more: mrclmb.ac.uk/news-events/... #LMBNews @cellbiol-mrclmb.bsky.social 🧪

Check out our latest paper on the ubiquitination of glycogen in cells and tissues! Congratulations to Marco Jochem (@marcojochem.bsky.social) and Simon Cobbold for leading this study and to collaborators @craigagoodman1.bsky.social, @pgregorevic.bsky.social, Kai Hofmann and Thomas Hermanns.

Marco Jochem@marcojochem.bsky.social · 5mo ago

Interested in non-proteinaceous ubiquitination, induced proximity or glycogen? Then you should have a look at our newest article, “Ubiquitination of glycogen and metabolites in cells and tissues”, just published in Nature: www.nature.com/articles/s41...

A new paper in which we could contribute structural insights to the great biochemical work from our collaborators from UNC Chapel Hill. Sascha Amann from our lab was yet again able to solve several very challenging structures. This time of a SCF with Protac and target www.nature.com/articles/s41...

IMP@impvienna.bsky.social · 5mo ago

Cells have a built-in cleanup system to remove unwanted proteins, and scientists can hijack it to destroy cancer drivers. Now, researchers from our Haselbach lab and collaborators reveal how this works in near-atomic detail: https://www.nature.com/articles/s41467-026-72235-9

Interested in non-proteinaceous ubiquitination, induced proximity or glycogen? Then you should have a look at our newest article, “Ubiquitination of glycogen and metabolites in cells and tissues”, just published in Nature: www.nature.com/articles/s41...

How do you get a charged drug into a cell when charged molecules can't cross the membrane? You don't — you let the cell do the charging. Check our new paper "Charged molecular glue discovery enabled by targeted degron display" in Nature Chemical Biology. ❕Publication: www.nature.com/articles/s41...

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

The E3 ubiquitin ligase mechanism specifying targeted microRNA degradation - Nature

Target-directed microRNA degradation is driven by the atypical ZSWIM8–CUL3 E3 ubiquitin ligase that uses a two-RNA-factor authentication mechanism to specifically recognize AGO–miRNA–trigger...

tinyurl.com

David Bartel's Lab@bartellab.bsky.social · 9mo ago

We are thrilled to share our latest work uncovering the mechanistic basis of target-directed microRNA degradation (TDMD). This work was driven by @jakobfarnung.bsky.social and @elenaslo.bsky.social in a fantastic collaboration with Brenda Schulman's lab. tinyurl.com/E3TDMD (1/5)

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

Jakob Farnung@jakobfarnung.bsky.social · 6mo ago

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...

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!

Leo Kiss@leokiss.bsky.social · 7mo ago

I am incredibly excited to share that I will start my independent lab at the @unidue-zmb.bsky.social at the @unidue.bsky.social as Junior Professor of Cellular Biochemistry. Research in my lab has the goal to decipher the ubiquitin code! There are multiple open positions! (1/3)

🚨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