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 - ThreadSky

haselbachlab.bsky.social • 23 days ago

New Preprint: We have solved the structure of the proteasome in complex with two different ubiquitin chains: https://www.biorxiv.org/content/10.1101/2025.04.07.647569v1 This work is spearheaded by PhD Student Sascha Amann
Let me walk you through it 🧵 1/9

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haselbachlab.bsky.social•23 days ago

Our collaborators @klanglab.bsky.social generated homogeneous tetraubiquitin chains with K48 linkage that could not be cleaved by the proteasome. 2/9

haselbachlab.bsky.social•23 days ago

This enabled us to solve the structure of a ubiquitin chain bound proteasome with cryoEM. All four ubiquitins are clearly visible. Unexpectedly, we see the ubiquitin chain wrap around the UIM1 motif of the ubiquitin receptor RPN10 in a spiral like fashion. 3/9

haselbachlab.bsky.social•23 days ago

The 4th ubiquitin is thereby having the most interactions explaining why it is this one that boosts the degradation at least in vitro. 4/9

haselbachlab.bsky.social•23 days ago

With our collaborator Nick Brown from UNC we were able to generate K11/K48 branched ubiquitin chains that are the chains predominantly used for cell cycle control. 5/9

haselbachlab.bsky.social•23 days ago

The K11 branch uses a new binding interface between RPN2 and RPN10, further ubiquitins of this branch are pointing towards the solution and may not further interact with the proteasome 6/9

haselbachlab.bsky.social•23 days ago

Finally, we tested the interfaces genetically with our collaborators in the @johanneszuber.bsky.social lab 7/9

selimlab.bsky.social•23 days ago

Congrats David!
Cool stuff....

haselbachlab.bsky.social•23 days ago

Thank you Khaled :)

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