Kai Gallant

From Pharmacophore to Warhead: NAD+‐Targeting Triazoles as Mechanism‐Based Sirtuin Inhibitors We report “Sirtuin Trapping Ligands” (SirTraps), mechanism-based 1,2,3-triazole inhibitors that hijack sirtuin (SIRT) catalysis to form covalent triazolium– or triazole–ADP-ribose (ADPR) adducts from...

We call these mechanism based sirtuin inhibitors SirTraps that trap the enzyme via this ADP ribose adduct onlinelibrary.wiley.com/doi/10.1002/... 2/

SAVE THE DATE!
The EMBO workshop "Ubiquitin and Ubiquitin-like proteins in Health and Disease" will be on September 2026.
Exciting line up of talks and an amazing location!
Organised by @kulathu.bsky.social, @merbllab.bsky.social, @simonapolo.bsky.social, Claudio Joazeiro.
Registration open soon.

🚨 Postdoc position in my lab!

A project on protein binder discovery for K6-linked #ubiquitin to investigate their role in infection is available.

📍 DTU, Copenhagen, Denmark
⏰ Deadline: 18 December 2025

Apply here: efzu.fa.em2.oraclecloud.com/hcmUI/Candid...

Join @uofglasgow.bsky.social for a funded 3.5 year PhD programme:

www.gla.ac.uk/colleges/mvl...

Also up for grabs is a project on antiviral PROTACs, supervised by us and the France lab (School of Chemistry) should ubiquitin and viruses appeal! Please get in touch with any questions.

Congrats Daniel 🎉

I supervise an excellent postdoc who's looking for a postdoc or associate position in < 1 yr. Highly skilled in chem biol and biochem (peptide synthesis, native chem ligation, bacterial expression, purification, intein-based splicing, crystallography, interaction assays). Contact me if interested.

Exciting news: We have released #FragPipe 23, and it's one of our biggest updates ever. Windows installer, support for TMT on Astral and timsTOF, TMT35, PTM site reports for DIA, improved Astral data handling in #MSFragger, improved diaTracer for diaPASEF data, better Skyline integration, and more!

Congrats to Nafizul for his fantastic Work, the passionate chemist @nikolasklink.bsky.social, skyless Gian and of course @maltegersch.bsky.social. It was a true pleasure to contribute to this Project 🌈

New Paper from the Lab 🎉If you are interested in USP30, protein engineering and targeting DUBs with small molecules I can wholeheartedly recommend this Paper 😊

A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia The temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using a multidisciplinary approach, we demonstrate that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts Hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis, and demonstrate how structural changes in IFT trains achieve cargo selectivity. ### Competing Interest Statement The authors have declared no competing interest. Sara Elizabeth O'Brien Trust Postdoctoral Fellowship awarded through the Charles A. King Trust Postdoctoral Research Fellowship Program, , 8460873-01 Richard and Susan Smith Family Foundation, https://ror.org/05j95n956, National Institute of General Medical Sciences (NIGMS), , R01GM141109, R01GM143183

How do cells keep their cilia “clean” and functional? Our new study uncovers a conserved mechanism for retrieving polyubiquitinated proteins from #cilia – a process essential for cellular signaling and health. #cellbiology #ciliopathy #ubiquitin #IFT 🧵👇 1/n

Super exiting new work revealing a novel quality control pathway for c-terminal amides!

From Dorothea Fiedler's lab: Protein polyphosphorylation as a new post-translational modification www.biorxiv.org/content/10.1...

🆕 #preprint by @gekaragoz.bsky.social lab & us on the crosstalk between #UFMylation & #RQC (ribosome-associated quality control) www.biorxiv.org/content/10.1... As always let us know what you think!

News in Proteomics Research blog post | Up to 5,300 proteins per actual single cell!?!? proteomicsnews.blogs...

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#proteomics #prot-other

W 3-Professur für Integrative Signalforschung - Albert-Ludwigs-Universität Freiburg Albert-Ludwigs-Universität Freiburg bietet Stelle als W 3-Professur für Integrative Signalforschung in Freiburg - jetzt bewerben!

Professorship Integrative Signaling Science. Freiburg, Germany. @cibss.bsky.social @biologyunifreiburg.bsky.social
www.academics.de/jobs/w-3-pro...

Thats a really cool Story and beautiful methodology! We recently discussed the effect of rewiring of E3s by glues and PROTACs in Journal Club and its nice to See that the question was Adressed so nicely✨Congrats to everyone involved

Who is messing with your favorite protein Filamin C in stressed muscle cells? 🧩🔬 We tackled this riddle in our latest paper in Scientific Reports. A huge shoutout to former lab mate Anja and Thomas from the @mkoehn.bsky.social lab - this was a true team effort! 👏🎉! A short thread: 🧵(1/5)

Such a beautiful story and elucidated mechanism! Congrats 🎉

Thank you for your kind words Loges! Hope you are having a fantastic time and to See U again soon 😊

A multivalent adaptor mechanism drives the nuclear import of proteasomes Nuclear protein homeostasis, including the turnover of transcription factors, critically depends on nuclear proteasomes. After each cell division, proteasomes need to be re-imported into the newly for...

We are very excited to share our recent preprint on the nuclear import mechanism of the proteasome, driven by the multivalent adaptor AKIRIN2! www.biorxiv.org/content/10.1... 🧵 1/6

I am very happy to have been part of the great team that made this story possible! Special thanks to my fabulous colleague Kim and @maltegersch.bsky.social and our collaborators in the @demmerslab.bsky.social!

Thrilled to share our study on the two DUBs USP53 and USP54! If you're curious about how biochemistry, chemical biology, crystallography, and ubiquitinated protein isolation came together to expand our understanding of these enzymes, consider to give it a read.

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Thank you! - i am really looking forward to the new Platform and Hope it will prosper🌻

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