Lorenz Lab

A Leishmania virulence factor harnesses an allosteric kinase switch to regulate its ubiquitin ligase activity Stringent control of ubiquitylation is a central requirement of signaling specificity in eukaryotes. Here, we discover a domain module integrating pro…

Allosteric activation of a ubiquitin ligase by an internal kinase domain! Congratulations to our team member Thornton Fokkens for this fascinating discovery in a neglected disease area with strong therapeutic need. Many thanks to all our great collaborators!
www.sciencedirect.com/science/arti...

Surprising tag: Scientists from @sonjalorenzlab.bsky.social and colleagues have now discovered that the human ligase HUWE1 can tag synthetic drug-like molecules in cells with ubiquitin. Their finding could open up new avenues in drug discovery and biotechnology.
@compbiophys.bsky.social

Join us - in person or online - for the Göttinger Literaturherbst, a literature festival with a unique science series. We will feature Katalin Karikó, among other research leaders.
Honoured to host Julian Nida-Rümelin on the pressing topic of democracy, 29 Oct.
www.mpinat.mpg.de/5094670/pr_2...

We’re excited that our article on the ubiquitination of drug-like small molecules in cells has been selected as an Editorial Highlight in #NatureCommun! 🎉
Check it out here 👉 www.nature.com/ncomms/edito...

Specifically, we reveal that compounds marketed as selective HUWE1 inhibitors are, in fact, efficient substrates of their target ligase, thus competing with protein substrates for ubiquitination in vitro.

We establish cellular detection methods, confirming HUWE1 promotes — but does not exclusively drive —compound ubiquitination in cells. This opens avenues for harnessing the ubiquitin system to transform synthetic small molecules into novel chemical modalities within cells.

Selective ubiquitination of drug-like small molecules by the ubiquitin ligase HUWE1 Nature Communications - Ubiquitination is a versatile modification system in eukaryotic cells. Here, the authors unveil that the ubiquitin ligase HUWE1 can modify drug-like small-molecule...

Delighted to share our work on cellular ubiquitination of drug-like compounds by HUWE1 - a surprising journey! Kudos to all contributors & first authors, Barbara Orth and Pavel Pohl. Sincere thanks to @ireserra.bsky.social ‬ #NatCommun for expertly guiding the winding publishing path.
rdcu.be/eDzPk

Policy Assistant, EMBO Policy Programme – EMBO Your role  As Policy Assistant, you will support the daily operations of the EMBO Policy Programme and contribute to projects on topics such as research assessment, research integrity, and science–pol...

Are you interested in a science policy career? Check out this interesting opening an EMBO! www.embo.org/vacancy/poli...

Congrats to our lab member, Sait! And thanks very much to all who supported his application! Looking forward to great discoveries to come.

Summer is now☀️, literature autumn next 🍂📖.
The program of the literature festival Göttinger Literaturherbst is out – and our scientific lecture series from Oct 24 to Nov 2 features brilliant Nobel Prize laureates, scientists, & non-fiction authors tackling big questions. Get your tickets!

Congratulations to our lab member, Dr. Thornton Fokkens, for his outstanding research, flawless PhD defense, and smooth climb to the Gänseliesel, the Göttingen landmark that is kissed by all new graduates!

Congratulations to our fantastic @mpi-nat.bsky.social student representatives at the Lindau Nobel Laureates Meeting! Have fun! #LINO25
Delighted that Rosi Junker from @sonjalorenzlab.bsky.social can attend. Many thanks to all supporters, including Brenda Schulman, @embo.org and GGNB Goettingen!

Europe’s choice is clear.

To put science at the heart of its economy.

To become the home of scientific freedom and collaboration.

And to welcome talent from all over the world.

I’m glad to present the first elements of our Choose Europe Initiative.

→ europa.eu/!TTbWbJ

NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome - Nature Structural & Molecular Biology Here, Arkinson et al. reconstitute NUB1-mediated FAT10 degradation by the human 26S proteasome and use biochemistry, cryo-EM and hydrogen–deuterium exchange to show that NUB1 acts as an ATP-independen...

We @natsmb.nature.com recently published an insightful manuscript on ubiquitin-independent proteasomal degradation via the NUB1-FAT10 axis by the lab of Andreas Martin. A very interesting read found here: www.nature.com/articles/s41...

Fantastic Ubiquitin CSH Meeting! Great science, reunion with old friends and many new contacts. Thanks to the master organizers: @annebertolotti.bsky.social, @labthoma.bsky.social, and Achim Werner!

Hi! Our lab has moved to Bluesky! We will discontinue our Twitter presence in the near future, so please watch out our news here!