Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5

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Protein complex prediction with AlphaFold-Multimer

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Fast and accurate protein structure search with Foldseek

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Fast and accurate protein structure search with Foldseek

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The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

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Atomic structures of respiratory complex III2, complex IV, and supercomplex III2-IV from vascular plants

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Greatwall Phosphorylates an Inhibitor of Protein Phosphatase 2Α That Is Essential for Mitosis

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The Substrate of Greatwall Kinase, Arpp19, Controls Mitosis by Inhibiting Protein Phosphatase 2A

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Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells

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Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

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Low-resolution refinement tools in REFMAC5

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B56‐containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX‐1 and ERK

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Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase

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A PP2A-B55 recognition signal controls substrate dephosphorylation kinetics during mitotic exit

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A PP1-PP2A phosphatase relay controls mitotic progression

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Integrator recruits protein phosphatase 2A to prevent pause release and facilitate transcription termination

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Microarray analysis of radiation response genes in primary human fibroblasts

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Predictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions

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Identification and functional characterization of transcriptional activators in human cells

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TRIP‐Br: a novel family of PHD zinc finger‐ and bromodomain‐interacting proteins that regulate the transcriptional activity of E2F‐1/DP‐1

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Protein phosphatase 2A as a therapeutic target in inflammation and neurodegeneration

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CDCA4 Is an E2F Transcription Factor Family-induced Nuclear Factor That Regulates E2F-dependent Transcriptional Activation and Cell Proliferation

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Inhibition of B56-containing Protein Phosphatase 2As by the Early Response Gene IEX-1 Leads to Control of Akt Activity

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Systematic Analysis of Human Protein Phosphatase Interactions and Dynamics

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IER5 generates a novel hypo-phosphorylated active form of HSF1 and contributes to tumorigenesis

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Protein Phosphatase 2A Controls the Order and Dynamics of Cell-Cycle Transitions

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Ier5,a Novel Member of the Slow-Kinetics Immediate-Early Genes

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PP2A-B55: substrates and regulators in the control of cellular functions

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Targeting PP2A for cancer therapeutic modulation

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Induced expression of the IER5 gene by γ-ray irradiation and its involvement in cell cycle checkpoint control and survival

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A minority of final stacks yields superior amplitude in single-particle cryo-EM

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Cryo-EM structures of PP2A:B55–FAM122A and PP2A:B55–ARPP19

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PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107

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FAM122A, a new endogenous inhibitor of protein phosphatase 2A

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HSF1 transcriptional activity is modulated by IER5 and PP2A/B55

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Isolation and Culture of Squamous Cell Carcinoma Lines

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Substrate recognition principles for the PP2A-B55 protein phosphatase

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Heat‐induced expression of the immediate‐early gene IER 5 and its involvement in the proliferation of heat‐shocked cells

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Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes

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IER5, a DNA damage response gene, is required for Notch-mediated induction of squamous cell differentiation

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Identification of PP2A as a novel interactor and regulator of TRIP-Br1

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Nuclear import of IER5 is mediated by a classical bipartite nuclear localization signal and is required for HSF1 full activation

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FAM122A ensures cell cycle interphase progression and checkpoint control by inhibiting B55α/PP2A through helical motifs

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Substrate recognition principles for the PP2A-B55 protein phosphatase

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Fuzziness in enzymatic catalysis

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The Fascinating Intricacy of pSer/Thr-Specific Phosphatases and Their Higher-Order Complexes: Emerging Concepts

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SERTAD1 is a novel substrate adapter for protein phosphatase 2A and induces site-specific dephosphorylation of heat shock factor 1

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Cryo-EM structures reveal the PP2A–B55α and Eya3 interaction that can be disrupted by a peptide inhibitor

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Structural and biochemical studies of human PP2A(B55) holoenzyme and ENSA protein complexPreprint

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Novel mechanism of substrate recognition by protein phosphatase PP2A:B55 involving SERTAD family adapter proteins

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SERTAD1 is a novel substrate adapter for protein phosphatase 2A and induces site-specific dephosphorylation of heat shock factor 1

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Regulation of CDC25B activity by protein phosphatase PP2A modulator IER5.

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Immediate‐early response 5 (IER5) interacts with protein phosphatase 2A and regulates the phosphorylation of ribosomal protein S6 kinase and heat shock factor 1

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I PP2A 1 Affects Tau Phosphorylation via Association with the Catalytic Subunit of Protein Phosphatase 2A

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Cryo-EM structures of PP2A:B55 with p107 and Eya3 define substrate recruitment

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