jake

@mediocre-jake.bsky.social

Postdoc interested in #ubiquitin #lipid #innateimmunity #E3ligases #endoplasmicreticulum https://findaresearcher.wehi.edu.au/chua.n Postdoc (WEHI) https://www.wehi.edu.au/laboratory/feltham-lab/ PhD (UNSW) https://x.com/brownlabunsw?lang=en&mx=

So delighted to have been part of this fantastic collaboration spearheaded by Ngee Kiat 'Jake' Chua (蔡毅杰) and Rebecca Feltham! Congratulations on bringing together so many experts in the field to make such an important resource 🎉 it has been a pleasure! www.sciencedirect.com/science/arti...

The E3-ome gene-centric compendium reveals the human E3 ligase landscape

To define and systematically characterize the human E3 ubiquitin ligase (E3) landscape, we generated the E3-ome, a compendium of E3s encoded by the hu…

sciencedirect.com

Amazing to be able to work with the team in Otago Many fundamental discoveries on what we know about RING E3s were made by Peter Mace at Catherine Day in New Zealand Always a pleasure to go back to basics and apply it with a modern lens @otagobiochemist.bsky.social

Otago Biochemistry@otagobiochemist.bsky.social · 4mo ago

Latest publication with a contribution from Otago Biochemistry. The E3-ome gene-centric compendium reveals the human E3 ligase landscape www.sciencedirect.com/science/arti...

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

Jakob Farnung@jakobfarnung.bsky.social · 5mo 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...

Ever wonder how IDRs and folded domains work together to control function? Using ubiquilins, multidomain proteins involved in protein degradation, we show in our new preprint that IDRs aren’t just linkers, but regulate ensemble and function. Read it here: doi.org/10.64898/202...

Intramolecular interactions between folded and disordered regions shape ubiquilin structure and function

Multidomain proteins consist of folded domains connected by intrinsically disordered regions. The flexibility afforded by the disordered regions coupled to the structure and surface chemistry of folded regions allows for unique structural and functional features in these proteins. Yet how intramolecular interactions between disordered regions and folded domains affect multidomain protein structure and function remain poorly understood. Here we use a range of biophysical and computational approaches to measure the intramolecular interactions between the folded domains and disordered regions of ubiquilins (UBQLNs) - essential components of protein quality control that shuttle poly-ubiquitinated client proteins to proteasomal degradation or autophagy. Starting with the yeast UBQLN homolog Dsk2, we find that interactions between two folded domains located at the opposite ends of UBQLN bring about a closed conformation. The prevalence of this closed conformation, however, is modulated by intramolecular interactions involving the disordered regions and folded STI1 domain at the center of the protein. Simulations and analysis of UBQLN homologs across multiple eukaryotic lineages reveals that these disordered:folded domain interactions exist in some UBQLN homologs but are absent in others, indicating possible fundamental differences in function among proteins with the same multidomain architecture. ### Competing Interest Statement The authors have declared no competing interest.

biorxiv.org

Scientists: How long have you waited for journal editors to decide whether the journal sends your manuscript out for review? I’m at 2+ months with a “prestigious” journal — not easy when working in a competitive field. What’s the longest you’ve experienced? #AcademicPublishing #PeerReview

Congratulations to the winners of this year's Art of Science Image contest at #bps2026 🥇 1st Place: Yupeng Li, University of Illinois Urbana-Champaign 🥈 2nd Place: Jessica Heebner, Thermo Fisher Scientific 🥉 3rd Place: Sohaib Abdul Rehman, Harvard University

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