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)
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
LLOMe has long been used to study lysosomal damage, yet how it works has remained a mystery.
Using cryo-electron tomography, we show it forms amyloid structures inside lysosomes that mechanically rupture membranes – revealing a new paradigm for lysosomal failure.
🔗 doi.org/10.64898/202...
#CryoET
New year, new preprint! 🎊
We are excited to share our recent work on #E3 ligase regulation in #metabolism!
www.biorxiv.org/content/10.6...
#ubiquitin #targetedproteindegradation #chemicalbiology
1/6
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).
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
A new paper reports the structure of the E4 enzyme Ufd2, which mediates K48 branched ubiquitination on K29diUb and K29triUb, identifying Ufd2’s core region as a K29diUb binding domain and a dimeric conformation for distal ubiquitin stabilization
www.nature.com/articles/s41...
Super excited to share our new #preprint on #BioRxiv ✨
We reveal the structural basis of a partnership between the ER membrane complex (EMC) and the P5A-ATPase Spf1 — an insertase–dislocase duo that coordinates membrane protein biogenesis and quality control.
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...
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
Thank you!
Check out our latest study @natsmb.nature.com: Establishing a consensus model for #ubiquitin chain assembly by HECT #E3 ligases: #cryoEM structures of #TRIP12 forming K29-linked and K29/K48-branched chains!
❕ www.nature.com/articles/s41...
@samuelmaiwald.bsky.social @unileiden.bsky.social
New online: TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains
Thank you Dawa! :)
Thank you Jakob! :)
Thanks Leo! :)
Many thanks to Brenda and all other coauthors from the Schulman lab @mpibiochem.bsky.social as well as our collaborators Matthew and Monique @unileiden.bsky.social, who made this work possible!
7/7
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
6/7
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
4/7
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
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...
@natsmb.nature.com
Many thanks to Brenda and all other coauthors from the Schulman lab @mpibiochem.bsky.social as well as our collaborators Matthew and Monique @unileiden.bsky.social, who made this work possible!
7/7
Comparison to our previous structure showing K48 chain formation by UBR5 suggests a consensus architecture for linkage-specific chain formation by HECT E3s.
6/7
On the other side, acceptor and donor ubiquitins come together with the TRIP12 HECT domain to establish the active site. Both sides cooperate to precisely place K29 of the proximal acceptor ubiquitin for catalysis.
5/7
One TRIP12 side avidly recruits the K48-linked chain, explaining preference for the proximal ubiquitin.
4/7
We used activity-based probes to trap TRIP12 in the act of forming a K29/K48-branched triUb and a K29-linked diUb. Visualizing these complexes using cryo-EM revealed TRIP12s catalytic mechanism.
3/7
TRIP12 adds K29-linked ubiquitin onto K48-linked ubiquitin chains. We show that TRIP12 preferentially modifies the proximal ubiquitin to form branched chains.
2/7
