Congratulations to first author Kasia Radziwon and co-authors Laura Campbell, Lauren Mazurkiewicz, Sopo Jalalshvili, Izabelle Eppinger, and Aanika Parikh! We are grateful to the NIH for supporting this work. Public investment in fundamental science fuels innovation and is worth defending.

Leveraging the throughput of our approach, we took a deep dive into the molecular basis of OspF specificity. We identified enzyme residues in the L12 loop that influence OspF’s specificity for pThr vs. pSer and were able to shift this specificity through protein engineering

We also found that the catalytic domain of the pThr lyase OspF (a functionally and mechanistically distinct phosphoeraser from Shigella flexneri) has and intrinsic preference for the pThr-Xaa-pTyr motif found in Erk and p38 MAP kinase activation loops that does not depend on its MAPK docking motif

We applied our approach to define sequence motifs for 8 phosphoerasers spanning diverse species, folds, and enzymatic mechanisms. Example: The Legionella pneumophila phosphatase WipB uses multiple selectivity filters, disfavoring substrates with Pro at +1 and phosphosites flanked by acidic residues

We developed an LC-MS/MS-based in vitro assay for dephosphorylation of human phosphoproteome-derived peptide libraries (PhosPropels). We use statistical comparison of phosphopeptide sequence features in enzyme-treated samples vs. controls for deep specificity profiling of phosphoeraser enzymes.

New preprint: we developed a method that uses phosphoproteome-derived peptide libraries (PhosPropels) for deep specificity profiling of phosphatases and phospholyases www.biorxiv.org/content/10.1...

We also found that the catalytic domain of the pThr lyase OspF (a functionally and mechanistically distinct phosphoeraser from Shigella flexneri) has and intrinsic preference for the pThr-Xaa-pTyr motif found in Erk and p38 MAP kinase activation loops that does not depend on its MAPK docking motif

We applied our approach to define sequence motifs for 8 phosphoerasers spanning diverse species, folds, and enzymatic mechanisms. Example: The Legionella pneumophila phosphatase WipB uses multiple selectivity filters, disfavoring substrates with Pro at +1 and phosphosites flanked by acidic residues

We developed an LC-MS/MS-based assay for dephosphorylation of human phosphoproteome-derived peptide libraries (PhosPropels). We use statistical comparison of phosphopeptide sequence features in enzyme-treated samples vs. controls for deep specificity profiling of phosphoerasers.

Congrats to Weeks lab graduate student Debashrito Deb @thepeptidetailor.bsky.social, who won a poster prize at the Bioorganic GRC last week! Thanks to conference chairs @doc-jlmeier.bsky.social and Denise Field who knocked it out of the park with a memorable and inspiring meeting this year!

My contribution to the Science Homecoming project--I wrote to The Item in Clinton, MA about the impacts that cuts to science funding will have on our health, our economy, and the opportunities available to young people in Clinton www.clintonitem.com/writes-cuts-...

@sciencehomecoming.bsky.social

Checking out the festive holiday decor at the Wisconsin State Capitol ☃️❄️

Grateful to work with this amazing team every day! ❄️📊🧪

Happy Holidays from the Weeks lab! This year's ornament is a working ferris wheel 🎡☃️

Excited to share some of our work at this upcoming CNPN-US HUPO ECR webinar! Register here: ushupo.org/Webinars #TeamMassSpec