ReviewTrends in biochemical sciences2023
Substrate and phosphorylation site selection by phosphoprotein phosphatases.
Review in Trends in biochemical sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed.
- Molecular Characterization of OsHAD Phosphoprotein: Expression, Catalytic Properties, and Functional Annotation.Molecular biotechnology · 2026Article
- SAPCD2 phosphorylation modulates astral microtubule stability to control spindle orientation.Communications biology · 2026Article
- Synthetic trap-peptides identify a TOM complex phosphatase - PP2A dephosphorylates Tom6.The FEBS journal · 2026Article
- Phosphatase specificity influences phosphorylation timing of CDK substrates during the cell cycle.Nature communications · 2025Article
- Research progress of SHP-1 agonists as a strategy for tumor therapy.Molecular diversity · 2025Review
- Cryo-EM structures of PP2A:B55 with p107 and Eya3 define substrate recruitment.Nature structural & molecular biology · 2025Article
- The Fascinating Intricacy of pSer/Thr-Specific Phosphatases and Their Higher-Order Complexes: Emerging Concepts.Biochemistry · 2025Review
- Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.Nature communications · 2025Article
- Dietary effects on the retina of hamsters.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- A chemical-genetic system to rapidly inhibit the PP2A-B56 phosphatase reveals a role at metaphase kinetochores.Nature communications · 2025Article
- Wnt signaling inhibits casein kinase 1α activity by modulating its interaction with protein phosphatase 2A.Cell reports · 2025Article
- Noncoding RNA-encoded peptides in cancer: biological functions, posttranslational modifications and therapeutic potential.Journal of hematology & oncology · 2025Review
- Identification of phosphatases that dephosphorylate the co-chaperone BAG3.Life science alliance · 2025Article
- The Role and Mechanism of Protein Post‑Translational Modification in Rheumatoid Arthritis.Journal of inflammation research · 2025Review
- The PNUTS phosphatase complex controls transcription pause release.Molecular cell · 2024Article
- 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
- Striatin plays a major role in angiotensin II-induced cardiomyocyte and cardiac hypertrophy in mice in vivo.Clinical science (London, England : 1979) · 2024Article
- Precise Orchestration of Gasdermins' Pore-Forming Function by Posttranslational Modifications in Health and Disease.International journal of biological sciences · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Dynamic protein phosphorylation and dephosphorylation are essential regulatory mechanisms that ensure proper cellular signaling and biological functions. Deregulation of either reaction has been implicated in several human diseases. Here, we focus on the mechanisms that govern the specificity of the dephosphorylation reaction. Most cellular serine/threonine dephosphorylation is catalyzed by 13 highly conserved phosphoprotein phosphatase (PPP) catalytic subunits, which form hundreds of holoenzymes by binding to regulatory and scaffolding subunits. PPP holoenzymes recognize phosphorylation site consensus motifs and interact with short linear motifs (SLiMs) or structural elements distal to the phosphorylation site. We review recent advances in understanding the mechanisms of PPP site-specific dephosphorylation preference and substrate recruitment and highlight examples of their interplay in the regulation of cell division.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.