ArticleNature communications2015
Centromeric binding and activity of Protein Phosphatase 4.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 50 citations in OpenAlex.
- Pervasive phenotypic effects of FBXO42 are promoted by regulation of PP4 phosphatase.The EMBO journal · 2026Article
- Asymmetry of centrosomes inMolecular biology of the cell · 2025Article
- Combining cryo-electron microscopy (cryo-EM) with orthogonal solution state methods to define the molecular basis of the phosphoprotein phosphatase family regulation and substrate specificity.Current opinion in structural biology · 2025Review
- SMEK1 ablation promotes glucose uptake and improves obesity-related metabolic dysfunction via AMPK signaling pathway.American journal of physiology. Endocrinology and metabolism · 2024Article
- Kin17 regulates proper cortical localization of Miranda in Drosophila neuroblasts by regulating Flfl expression.Cell reports · 2024Article
- Article
- Identification of protein phosphatase 4 catalytic subunit as a Wnt promoting factor in pan-cancer and Xenopus early embryogenesis.Scientific reports · 2023Article
- Nuclear-enriched protein phosphatase 4 ensures outer kinetochore assembly prior to nuclear dissolution.The Journal of cell biology · 2023Article
- GST-IVTT pull-down: a fast and versatile in vitro method for validating and mapping protein-protein interactions.FEBS open bio · 2022Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022Review
- Protein Phosphatase 4 Negatively Regulates the Immune Deficiency-NF-κB Pathway during theJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- Novel perspectives of target-binding by the evolutionarily conserved PP4 phosphatase.Open biology · 2020Article
- A fraction of barrier-to-autointegration factor (BAF) associates with centromeres and controls mitosis progression.Communications biology · 2020Article
- Functional roles of protein phosphatase 4 in multiple aspects of cellular physiology: a friend and a foe.BMB reports · 2020Review
- Leveraging New Definitions of the LxVP SLiM To Discover Novel Calcineurin Regulators and Substrates.ACS chemical biology · 2019Article
- A Consensus Binding Motif for the PP4 Protein Phosphatase.Molecular cell · 2019Article
- Review
- PP4 deficiency leads to DNA replication stress that impairs immunoglobulin class switch efficiency.Cell death and differentiation · 2019Article
- PLATINUM SENSITIVE 2 LIKE impacts growth, root morphology, seed set, and stress responses.PloS one · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.
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.