Hofmann_Lab
@LabHofmann
Research group at the University of Cologne
Our paper on bacterial clippases is now out in @MolecularCell. These really interesting enzymes can make deconjugation of #ubiquitin irreversible. Thanks to @UniCologne and @C2fBiochemistry for support. cell.com/molecular-cell…
New Parkinson’s disease paper: Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of USP30 and a framework for DUB ligandability - published by @MalteGersch group @maxplanckpress in @Nature Struct. & Mol. Biol. nature.com/articles/s4159…
Excited to share that our work on Parkinson's target USP30 has been published in Nature Structural & Molecular Biology! By combining DUB-domains onto USP30, we for the first time achieved crystallization with a small molecule (NK036) without Nanobodies! nature.com/articles/s4159…
Congratulations, great paper! But what makes you think that this is a CARD and not just any death-fold domain? pyrin and DEDs can also activate caspases and invertebrates use all kinds of death-fold domains for that purpose! I don't think this one really should be called CARD.
We previously showed that bacteria encode the pore-forming protein gasdermin and that it defends against phage infection science.org/doi/10.1126/sc… BUT the mechanism by which the gasdermin system defends bacteria against phage remained unknown.
Great paper, but sorry, this is *not* a CARD domain! It is a 6-helix death fold domain for sure, but there in no evidence provided that it belongs to the CARD subfamily. It might have (convergently?) acquired a similar function as mammalian caspase-associated CARDs. Just saying.
Our paper out @Nature: CARD domains mediate anti-phage defense in bacterial gasdermin systems CARDs are essential for caspase recruitment in inflammasome activation. We now find them in bacterial immune systems Congrats @TanaWein! Thanks Kranzusch lab! tinyurl.com/CA88DD
Very excited to share that our manuscript on the "Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53" was published today at Nature Chemical Biology @nchembio. Congratulations Kim, Kai, and all authors! nature.com/articles/s4158…
For all ubiquitin, deubiquitinase and chemical biology aficionados: Here's a preprint from the lab introducing 2 new active DUBs in humans & a unique type of DUB activity one would miss with the widely used panels of free ubiquitin chains. t.ly/GnRVv Thread👇(1/10)
New Lammers Lab paper out now in @NatureComms!🥳 We reveal high functional diversity within bacterial deac(et)ylases by systematic functional/structural characterization. This is Leonies PhD project and I’m grateful to have contributed to this great work. nature.com/articles/s4146…
Endlessly fascinating and exciting conference with great discussions #EMBOubiquitin24 ! Can’t wait to get back to the lab with some new ideas…
After a long time in the making, our study on bacterial clippases is finally available as a preprint biorxiv.org/content/10.110… These are really fascinating enzymes, for which there will be a ton of applications in studying the #ubiquitin system
Recent reports implicated USP53 mutations in a hereditary liver disorder in children. We got interested in USP53 and its homologue USP54 as phylogenetically they are the most diverse USP DUB family members but according to uniprot are supposed to be catalytically inactive.(2/10)
N4BP1 functions as a dimerization-dependent linear #ubiquitin reader which regulates TNF signalling nature.com/articles/s4142…
Two PhD positions in our research group! If you are interested to study the molecular mechanisms of necroptotic and pyroptotic cell death - and their relationship to plant cell death, do apply!
Do you love #genetics and have a #MSc in #biochemistry, #biology, or #biophysics? 🧬🌱Join @UniCologne in Germany as #research assistant in the @dfg_public-funded network @sfb_1403 on cell death in immunity, inflammation & disease! Apply by 04/02: stellenwerk.de/koeln/jobboers…
By the way: this project was the brainchild of excellent postdoc Thomas Hermanns, who was also corresponding author! We also acknowlegde support from @C2fBiochemistry and @UniCologne
Now published: We analyzed the structure of the Burkholderia effector TssM with and without ubiquitin. TssM is a divergent member of the USP-type deubiquinases and can recognize #ubiquitin despite the lack of the 'fingers' domain. life-science-alliance.org/content/7/2/e2…
Now published: We analyzed the structure of the Burkholderia effector TssM with and without ubiquitin. TssM is a divergent member of the USP-type deubiquinases and can recognize #ubiquitin despite the lack of the 'fingers' domain. life-science-alliance.org/content/7/2/e2…
Congratulations, Tyler & Jonathan, great work!
Excited to share the final product of this work, now available at @MolecularCell. Extremely proud of @tylergfranklin for this and many other achievements during his thesis work! sciencedirect.com/science/articl…
Out now in NatComms: A Chlamydia-like bacterium with a deubiquitinase repertoire similar to Legionella, but using new DUB classes for the same linkage specificities (e.g. M1, K6). #ubiquitin @UniCologne @C2fBiochemistry doi.org/10.1038/s41467…
Our new manuscript on Burkholderia TssM is on bioRxiv. TssM is an interesting bacterial USP-type dubiquitinase effector, which lacks the so-called 'Fingers' Region used by other USPs for #ubiquitin recognition. Our structures show how TssM does the trick biorxiv.org/content/10.110…
Nice poster!
last weeks @BiochemSoc conference on #DUBs and #Ubls in Edinburgh was a blast! lots of new and interesting aspects all around #ubiquitin erasers from molecular basics to applications. thanks to all organizers for putting together this great #biochemevent, see you next time! 🤩
DUBS 2023 will bring together leading academic researchers in the DUB/ULP area with their counterparts in biotech and pharma to initiate, and advance collaborative research. Register now and join us on 19-21 June: bit.ly/DUBS-2023