Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, Caroline; Haesen, Dorien; Sents, Ward; Ivanova, Elitsa; Janssens, Veerle

doi:10.1007/978-1-62703-562-0_17

Cited by 140Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, Caroline, Haesen, Dorien, Sents, Ward, Ivanova, Elitsa, Janssens, Veerle·2013·Methods in Molecular Biology

DOI 10.1007/978-1-62703-562-0_17

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Abstract

Protein phosphatases of the type 2A family (PP2A) represent a major fraction of cellular Ser/Thr phosphatase activity in any given human tissue. In this review, we describe how the holoenzymic nature of PP2A and the existence of several distinct PP2A composing subunits allow for the generation of multiple structurally and functionally different PP2A complexes, explaining why PP2A is involved in the regulation of so many diverse cell biological and physiological processes. Moreover, in human disease, most notably in several cancers and Alzheimer's Disease, PP2A expression and/or activity have been found significantly decreased, underscoring its important functions as a major tumor suppressor and tau phosphatase. Hence, several recent preclinical studies have demonstrated that pharmacological restoration of PP2A activity, as well as pharmacological PP2A inhibition, under certain conditions, may be of significant future therapeutic value.

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CIP2A is the most prevalent oncoprotein among PP2A inhibitor proteins.
“Among them, cancerous inhibitor of PP2A (CIP2A) is the most prevalent oncoprotein”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [8]
The therapeutic effects of inhibition of CIP2A protein expression have been validated by numerous studies.
“This is a very important finding because the therapeutic effects of inhibition of CIP2A protein expression have been validated by numerous studies [6 -8,10 -12,21].”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [8]
PP2A is a family of Ser/Thr phosphatases made of a catalytic C subunit and a structural A subunit, usually bound to a regulatory B-type subunit.
“Protein Phosphatase 2A (PP2A) encompasses a large family of Ser/Thr phosphatases, consisting of a catalytic C subunit and a structural A subunit that are, in most cases, further bound to a regulatory B-type subunit.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [6]
In mammals, the C and A subunits are each encoded by two genes, producing α and β isoforms.
“In mammals, both subunits are each encoded by two distinct genes, leading to an α and β protein isoform.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [6]

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Dihydroxyphenylethanol induces apoptosis by activating serine/threonine protein phosphatase PP2A and promotes the endoplasmic reticulum stress response in human colon carcinoma cells
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A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivoPreprint
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The Protein Phosphatase 2A Phosphatase Activator Is a Novel Peptidyl-Prolyl cis/trans-Isomerase
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Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster
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Purification and Characterization of a Novel Xylulose 5-Phosphate-activated Protein Phosphatase Catalyzing Dephosphorylation of Fructose-6-phosphate,2-kinase:Fructose-2,6-bisphosphatase
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An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator
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Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein
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The protein phosphatases involved in cellular regulation
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Vimentin Dephosphorylation by Protein Phosphatase 2A Is Modulated by the Targeting Subunit B55
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Human cancer-associated mutations in the Aα subunit of protein phosphatase 2A increase lung cancer incidence in Aα knock-in and knockout mice
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cAMP-stimulated Protein Phosphatase 2A Activity Associated with Muscle A Kinase-anchoring Protein (mAKAP) Signaling Complexes Inhibits the Phosphorylation and Activity of the cAMP-specific Phosphodiesterase PDE4D3
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The Effects of Cantharidin and Cantharidin Derivates on Tumour Cells
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The Role and Therapeutic Potential of Ser/Thr Phosphatase PP2A in Apoptotic Signalling Networks in Human Cancer Cells
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A Developmentally Regulated, Neuron-specific Splice Variant of the Variable Subunit Bβ Targets Protein Phosphatase 2A to Mitochondria and Modulates Apoptosis
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Generation of Active Protein Phosphatase 2A Is Coupled to Holoenzyme Assembly
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APOE-Mimetic Peptides Reduce Behavioral Deficits, Plaques and Tangles in Alzheimer’s Disease Transgenics
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The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little resemblance to T antigens
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Misshapen-like kinase 1 (MINK1) Is a Novel Component of Striatin-interacting Phosphatase and Kinase (STRIPAK) and Is Required for the Completion of Cytokinesis
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Identification of a PP2A-interacting protein that functions as a negative regulator of phosphatase activity in the ATM/ATR signaling pathway
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Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling
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Molecular Cloning and Characterization of Phocein, a Protein Found from the Golgi Complex to Dendritic Spines
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Cacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsy
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Effects of Phosphorylation of Immunomodulatory Agent FTY720 (Fingolimod) on Antiproliferative Activity against Breast and Colon Cancer Cells
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Striatin, a calmodulin‐dependent scaffolding protein, directly binds caveolin‐1
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Structure-Activity Relationship Studies of Fostriecin, Cytostatin, and Key Analogs, with PP1, PP2A, PP5, and (β12–β13)-Chimeras (PP1/PP2A and PP5/PP2A), Provide Further Insight into the Inhibitory Actions of Fostriecin Family Inhibitors
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Lithium Inhibits Ceramide- and Etoposide-Induced Protein Phosphatase 2A Methylation, Bcl-2 Dephosphorylation, Caspase-2 Activation, and Apoptosis
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Protein Phosphatase 2A as a Potential Target for Anticancer Therapy
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Genomic organisation, chromosomal localisation tissue distribution and developmental regulation of the PR61/B′ regulatory subunits of protein phosphatase 2A in mice
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Functions of B56-containing PP2As in major developmental and cancer signaling pathways
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Diversity, developmental regulation and distribution of murine PR55/B subunits of protein phosphatase 2A
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ATM-mediated phosphorylation activates the tumor-suppressive function of B56γ–PP2A
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FTY720 Shows Promising In vitro and In vivo Preclinical Activity by Downmodulating Cyclin D1 and Phospho-Akt in Mantle Cell Lymphoma
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Generation of Ppp2Ca and Ppp2Cb conditional null alleles in mouse
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Molecular cloning of a 74‐kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A
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Identification of in vivo phosphorylation sites of SET, a nuclear phosphoprotein encoded by the translocation breakpoint in acute undifferentiated leukemia
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The Apolipoprotein-E-Mimetic COG112 Protects Amyloid Precursor Protein Intracellular Domain-Overexpressing Animals from Alzheimer's Disease-Like Pathological Features
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Protein Phosphatase Inhibition: Structure Based Design. Towards New Therapeutic Agents
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Troglitazone acutely inhibits protein synthesis in endothelial cells via a novel mechanism involving protein phosphatase 2A-dependent p70 S6 kinase inhibition
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Crystal Structure of the PP2A Phosphatase Activator: Implications for Its PP2A-Specific PPIase Activity
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PP2A and Alzheimer Disease
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Rubratoxin A specifically and potently inhibits protein phosphatase 2A and suppresses cancer metastasis
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Dithiolethione compounds inhibit Akt signaling in human breast and lung cancer cells by increasing PP2A activity
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Specific inhibitors of protein phosphatase 2A inhibit tumor metastasis through augmentation of natural killer cells
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Protein phosphatase 2A is targeted to cell division control protein 6 by a calcium-binding regulatory subunit
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Protein phosphatase 2A PR130/B”α:1 subunit binds to the SH2 domain‐containing inositol polyphosphate 5‐phosphatase 2 and prevents epidermal growth factor (EGF)‐induced EGF receptor degradation sustaining EGF‐mediated signaling
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The B56γ3 Regulatory Subunit of Protein Phosphatase 2A (PP2A) Regulates S Phase-specific Nuclear Accumulation of PP2A and the G1 to S Transition
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Sphingosine Interaction with Acidic Leucine-rich Nuclear Phosphoprotein-32A (ANP32A) Regulates PP2A Activity and Cyclooxygenase (COX)-2 Expression in Human Endothelial Cells
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MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR
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A B56 regulatory subunit of protein phosphatase 2A localizes to nuclear speckles in cardiomyocytes
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Targeting phosphatases as the next generation of disease modifying therapeutics for Parkinson’s disease
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Authors: Lambrecht, C., Haesen, D., Sents, W., Ivanova, E., & Janssens, V.
Affiliations: KU Leuven (BE)
ORCID: Ivanova, Elitsa
Janssens, Veerle
Venue: Methods in Molecular Biology
Publisher: Humana Press
Published: 2013
Volume: 1053
Pages: 283-305
ISSN: 1064-3745 (ISSN-L)
1940-6029
DOI: 10.1007/978-1-62703-562-0_17
OpenAlex: W151043947
Cited by: 140
References: 171
Citations by year: 2026: 6 · 2025: 9 · 2024: 4 · 2023: 16 · 2022: 16 · 2021: 13 · 2020: 7 · 2019: 10 · 2018: 7 · 2017: 14 · 2016: 21 · 2015: 3 · 2014: 12 · 2013: 2
FWCI: 16.61
Type: book chapter
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Methods in molecular biology (publishedVersion)
PubMed (publishedVersion)
Lirias (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: protein phosphatase 2A, PP2A regulatory subunit, serine/threonine phosphatase, tumor suppressor, Alzheimer's disease, cancer, PP2A inhibitors
MeSH terms: Alzheimer Disease, Enzyme Inhibitors, Humans, Isoenzymes, Neoplasms, Holoenzymes, Enzyme Activators, Protein Phosphatase 2

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Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

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