ArticleMolecular systems biology2023
Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification.
Article in Molecular systems biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 20 citations in OpenAlex.
- Decoupling Fabrication From Encoding: DNA-Addressable Template Microparticles for Large, User-Defined Optical Barcode Libraries.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Amplicon/Protein Bead Display enables quantitativebioRxiv : the preprint server for biology · 2026Article
- Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.STAR protocols · 2026Article
- Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- FAM122A inhibition of PP2A-B55 through a bipartite binding mechanism.bioRxiv : the preprint server for biology · 2026Article
- Switching of the c-Myc protein degradation pathway depending on the PP2A-B55α complex levels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The balance between B55α and Greatwall expression levels predicts sensitivity to Greatwall inhibition in cancer cells.Nature communications · 2025Article
- Combination of in vivo and in vitro phosphoproteomics determines the PP2A target repertoire on proteome scale.Cell reports methods · 2025Article
- The Fascinating Intricacy of pSer/Thr-Specific Phosphatases and Their Higher-Order Complexes: Emerging Concepts.Biochemistry · 2025Review
- Wnt signaling inhibits casein kinase 1α activity by modulating its interaction with protein phosphatase 2A.Cell reports · 2025Article
- Identification of phosphatases that dephosphorylate the co-chaperone BAG3.Life science alliance · 2025Article
- GPSD: a hybrid learning framework for the prediction of phosphatase-specific dephosphorylation sites.Briefings in bioinformatics · 2024Article
- A protein phosphatase 1 specificProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Substrate recognition principles for the PP2A-B55 protein phosphatase.Science advances · 2024Article
- Phosphoproteomic investigation of targets of protein phosphatases in EGFR signaling.Scientific reports · 2024Article
- Article
- Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification.Molecular systems biology · 2023Article
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Phosphoprotein phosphatases (PPPs) regulate major signaling pathways, but the determinants of phosphatase specificity are poorly understood. This is because methods to investigate this at scale are lacking. Here, we develop a novel in vitro assay, MRBLE:Dephos, that allows multiplexing of dephosphorylation reactions to determine phosphatase preferences. Using MRBLE:Dephos, we establish amino acid preferences of the residues surrounding the dephosphorylation site for PP1 and PP2A-B55, which reveals common and unique preferences. To compare the MRBLE:Dephos results to cellular substrates, we focused on mitotic exit that requires extensive dephosphorylation by PP1 and PP2A-B55. We use specific inhibition of PP1 and PP2A-B55 in mitotic exit lysates coupled with phosphoproteomics to identify more than 2,000 regulated sites. Importantly, the sites dephosphorylated during mitotic exit reveal key signatures that are consistent with MRBLE:Dephos. Furthermore, integration of our phosphoproteomic data with mitotic interactomes of PP1 and PP2A-B55 provides insight into how binding of phosphatases to substrates shapes dephosphorylation. Collectively, we develop novel approaches to investigate protein phosphatases that provide insight into mitotic exit regulation.
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