ReviewThe Biochemical journal2018
The split protein phosphatase system.
Review in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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
38 citing papers in PubMed, 58 citations in OpenAlex.
- Selective Hydroxylation of Collagen Model Peptides by Metal Catalysis.Chemistry & biodiversity · 2026Article
- Termination of the integrated stress response.Science (New York, N.Y.) · 2026Article
- AMPK-PP1/PP2 axis regulates GSDMD-mediated pyroptosis via phosphorylation.Frontiers in oncology · 2026Article
- Potential Role of the Glycogen-Targeting Phosphatase Regulatory Subunit in Airway Hyperresponsiveness in Asthma.Biomedicines · 2025Article
- ASPPs multimerize protein phosphatase 1.PLoS genetics · 2025Article
- Combination of in vivo and in vitro phosphoproteomics determines the PP2A target repertoire on proteome scale.Cell reports methods · 2025Article
- Phosphorylation of a nuclear condensate regulates cohesion and mRNA retention.Nature communications · 2025Article
- Article
- Integrated stress response activator halofuginone protects mice from diabetes-like phenotypes.The Journal of cell biology · 2024Article
- Collective cell migration relies on PPP1R15-mediated regulation of the endoplasmic reticulum stress response.Current biology : CB · 2024Article
- Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B.Molecular cell · 2024Article
- The PPP1R15 Family of eIF2-alpha Phosphatase Targeting Subunits (GADD34 and CReP).International journal of molecular sciences · 2023Review
- Protein phosphatase 1 regulates core PCP signaling.EMBO reports · 2023Article
- Activation of the integrated stress response by inhibitors of its kinases.Nature communications · 2023Article
- Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer.International journal of molecular sciences · 2023Review
- Functional Metagenomics Approach for the Discovery of Novel Genes Encoding Phosphatase Activity.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Protein Targeting to Glycogen (PTG): A Promising Player in Glucose and Lipid Metabolism.Biomolecules · 2022Review
- The Caenorhabditis elegans ASPP homolog APE-1 is a junctional protein phosphatase 1 modulator.Genetics · 2022Article
- Temporal and thermal profiling of theeLife · 2022Article
- Cellular responses to halofuginone reveal a vulnerability of the GCN2 branch of the integrated stress response.The EMBO journal · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Reversible phosphorylation of proteins is a post-translational modification that regulates all aspect of life through the antagonistic action of kinases and phosphatases. Protein kinases are well characterized, but protein phosphatases have been relatively neglected. Protein phosphatase 1 (PP1) catalyzes the dephosphorylation of a major fraction of phospho-serines and phospho-threonines in cells and thereby controls a broad range of cellular processes. In this review, I will discuss how phosphatases were discovered, how the view that they were unselective emerged and how recent findings have revealed their exquisite selectivity. Unlike kinases, PP1 phosphatases are obligatory heteromers composed of a catalytic subunit bound to one (or two) non-catalytic subunit(s). Based on an in-depth study of two holophosphatases, I propose the following: selective dephosphorylation depends on the assembly of two components, the catalytic subunit and the non-catalytic subunit, which serves as a high-affinity substrate receptor. Because functional complementation of the two modules is required to produce a selective holophosphatase, one can consider that they are split enzymes. The non-catalytic subunit was often referred to as a regulatory subunit, but it is, in fact, an essential component of the holoenzyme. In this model, a phosphatase and its array of mostly orphan substrate receptors constitute the split protein phosphatase system. The set of potentially generalizable principles outlined in this review may facilitate the study of these poorly understood enzymes and the identification of their physiological substrates.
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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.