Research group at the University of Cologne
Joined July 2020
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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/full…
Hofmann_Lab retweeted
Proud to share The E3-ome
A true collaborative effort to unify the human E3 ligase landscape, and create a shared foundation for the field
#Ubiquitin #E3Ligases @WEHI_research
cell.com/cell/fulltext/S0092…
I am deeply saddened learning that my scientific hero Amos Bairoch has recently passed away. He will be remembered as the mastermind behind the SwissProt and many other endeavours in protein bioinformatics. There is a tribute web page at sib.swiss/amos/
For all #ubiquitin aficionados out there: Our new study, where we used an #alphafold based screen and found a new class of plant-specific DUBs, which cleave K63 chains and interfere with endocytosis at the plasma membrane. biorxiv.org/content/10.64898…
Very interesting finding from the Escobar group next door, with some minor contributions from us.
Online Now: Ubiquitin precursor with C-terminal extension promotes proteostasis and longevity dlvr.it/TNFK9q
Hofmann_Lab retweeted
Measure protein deamidation by bacterial secreted proteins? Check out the recent NMR paper. Congratulations to @Rashmi_Agrata
doi.org/10.1002/mrc.70045
Hofmann_Lab retweeted
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/s41594-0…
Hofmann_Lab retweeted
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/s41594-0…
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/scie…
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
Hofmann_Lab retweeted
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/s41589-0…
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)
Hofmann_Lab retweeted
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/s41467-0…
Hofmann_Lab retweeted
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/10.1101/…
These are really fascinating enzymes, for which there will be a ton of applications in studying the #ubiquitin system
Hofmann_Lab retweeted
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/s41420-0…
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/jobboer…
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/co…
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/co…