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Showing ARPP19 — ARPP-16 is a alias.

ARPP19

cAMP-regulated phosphoprotein 19 · UniProt P56211

Length
112 aa
Mass
12.3 kDa
Annotated
2026-06-09
38 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ARPP19 is an intrinsically disordered protein that functions as a regulatable inhibitor of protein phosphatase PP2A, integrating opposing kinase inputs to control the timing of mitotic and meiotic transitions (PMID:21164014, PMID:24525567). Upon phosphorylation at S67 by Greatwall kinase, ARPP19 binds PP2A-B55δ and inhibits its activity, sustaining Cdk1 activation and driving M-phase entry; this step is essential within the Cdk1 auto-amplification loop (PMID:21164014, PMID:23781026). The phospho-S67 mark confers high affinity and slow dephosphorylation kinetics, allowing ARPP19 to act as a competitive inhibitor of PP2A-B55 substrates, and cryo-EM and NMR show the disordered protein engages multiple distinct sites on the B55 subunit (PMID:34117214, PMID:38123684). A second, antagonistic input is provided by PKA, which phosphorylates ARPP19 at S109 to maintain prophase arrest in oocytes; this PKA site is itself dephosphorylated by PP2A-B55δ to initiate meiotic resumption, and reciprocal feedback between S67 and S109 coordinates phosphatase inhibition with Cyclin B/Cdk1 activation (PMID:24525567, PMID:34117214, PMID:33758202). ARPP19 is genetically essential for mouse embryogenesis and for proper mitotic dephosphorylation timing, a role its paralog ENSA cannot substitute (PMID:30626720). A Cdk1-dependent S23 phosphorylation, removed by Fcp1 at mitotic exit, tunes the timing of exit and safeguards chromosome segregation (PMID:40447768). The striatum-enriched isoform ARPP-16 is phosphorylated at S46 by MAST3 to inhibit PP2A and is opposed by PKA-mediated S88 phosphorylation, establishing a cAMP-regulated switch governing PP2A activity in neurons (PMID:28167675, PMID:28613156). Beyond cell-cycle control, ARPP-19 binds the 3' region of GAP-43 mRNA in a PKA-phosphorylation-dependent manner to regulate its stability downstream of NGF (PMID:12221279).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1990 Medium

    Established ARPP-16/ARPP-19 as a pair of PKA substrates differing only by an N-terminal extension, defining the protein and its regulatory phosphoacceptor.

    Evidence Protein purification, cDNA cloning, and in vitro PKA phosphorylation assays

    PMID:2160982

    Open questions at the time
    • No cellular function assigned at this stage
    • Phosphatase target PP2A not yet identified
  2. 2001 Medium

    Linked ARPP phosphorylation to dopamine receptor signaling, showing PKA-site phosphorylation is dynamically regulated by D1/D2 receptor activity in striatum.

    Evidence In vitro kinase assays, phospho-specific immunoblotting, and striatal slice pharmacology

    PMID:11279279

    Open questions at the time
    • Downstream effector of phosphorylated ARPP unknown
    • No mechanistic link to PP2A yet
  3. 2002 Medium

    Revealed an RNA-regulatory role distinct from phosphatase control, showing PKA-phosphorylated ARPP-19 binds GAP-43 mRNA to control its stability under NGF.

    Evidence RNA-protein binding, 3'UTR reporter assays, and phospho-site mutagenesis in PC12 cells

    PMID:12221279

    Open questions at the time
    • RNA-binding determinants not mapped
    • Generality beyond GAP-43 mRNA untested
    • Relation to PP2A function unresolved
  4. 2010 High

    Defined ARPP19's core mitotic function: Greatwall-phosphorylated ARPP19 inhibits PP2A to promote mitotic entry, with endogenous ARPP19 (not ENSA) responsible in egg extracts.

    Evidence Greatwall-substrate identification, co-IP, and depletion/add-back in Xenopus egg extracts

    PMID:21164014

    Open questions at the time
    • Specific phosphosite and PP2A holoenzyme not yet pinned down
    • Structural basis of inhibition unknown
  5. 2013 High

    Identified S67 as the Greatwall site and PP2A-B55δ as the target, placing ARPP19 inside the Cdk1 auto-amplification loop and showing S67 phosphorylation escapes PKA control.

    Evidence Phospho-mutant analysis, PP2A activity assays, and co-IP in Xenopus oocytes

    PMID:23781026

    Open questions at the time
    • Kinetic basis of inhibition not quantified
    • Crosstalk with the PKA site mechanistically undefined
  6. 2014 High

    Established the antagonistic PKA arm: S109 phosphorylation maintains prophase arrest, and progesterone-driven partial dephosphorylation permits Cdk1 activation, positioning ARPP19 as an integrator of PKA and Greatwall signals.

    Evidence S109A/S109D phospho-mutants, kinase assays, and PKA manipulation in Xenopus oocytes

    PMID:24525567

    Open questions at the time
    • Phosphatase removing S109 not yet identified
    • Quantitative coupling of S67 and S109 unresolved
  7. 2017 High

    Extended the model to neurons, showing MAST3 phosphorylates ARPP-16 at S46 to selectively inhibit B55α/B56δ-PP2A, with PKA at S88 opposing this, defined by direct A-subunit interaction and a conditional-KO substrate phenotype.

    Evidence In vitro kinase assays, co-IP, and CaMKIIα::cre conditional ARPP-16/19 knockout mouse with phospho-substrate readouts

    PMID:28167675

    Open questions at the time
    • Full set of neuronal PP2A substrates incomplete
    • Physiological/behavioral consequences not fully mapped
  8. 2017 High

    Resolved the PKA-MAST3 logic as a mutually suppressive, switch-like circuit controlling neuronal PP2A activity in response to cAMP.

    Evidence In vitro kinase assays, mass spectrometry, phospho-mutants, and mathematical modeling

    PMID:28613156 PMID:28722544

    Open questions at the time
    • In vivo demonstration of switch dynamics limited
    • Cell-cycle vs neuronal Greatwall/MAST3 division of labor not unified
  9. 2019 High

    Demonstrated genetic necessity and non-redundancy: ARPP19 is essential for embryogenesis and mitotic dephosphorylation timing, while ENSA acts in S phase, separating paralog functions.

    Evidence Conditional Arpp19 and Ensa knockout mice with MEF viability and cell-cycle phospho-timing analyses

    PMID:30626720

    Open questions at the time
    • Molecular basis of ARPP19/ENSA functional divergence unclear
    • S-phase mechanism of ENSA not addressed for ARPP19
  10. 2021 High

    Provided the kinetic and feedback mechanism: phospho-S67 confers slow-turnover competitive inhibition of PP2A-B55, S109 restricts S67 via accelerated dephosphorylation, and PP2A-B55δ dephosphorylates S109 to release prophase arrest.

    Evidence In vitro phosphatase kinetics, binding affinity measurements, phospho-mutants, and Xenopus extract/oocyte reconstitution

    PMID:33758202 PMID:34117214

    Open questions at the time
    • Atomic-level basis of multivalent binding not yet visualized
    • Regulation of PP2A-B55δ dual targeting of S67 vs S109 incompletely defined
  11. 2021 Medium

    Characterized ARPP19/ARPP-16 as intrinsically disordered proteins engaging PP2A through a linear A-subunit motif plus weak multivalent B56 contacts, framing the structural basis of recognition.

    Evidence NMR, SAXS, and microscale thermophoresis binding measurements

    PMID:33842550

    Open questions at the time
    • Affinity in isolation is modest; phospho-dependent contacts not fully resolved
    • Functional weight of individual motifs untested
  12. 2023 High

    Delivered the structural mechanism: cryo-EM and NMR show phospho-ARPP19 occupies multiple distinct B55 sites, explaining how PP2A:B55 recruits both substrates and inhibitors.

    Evidence Single-particle cryo-EM, NMR, and biophysical assays of PP2A:B55-ARPP19

    PMID:38123684

    Open questions at the time
    • Dynamics of the disordered regions in the complex not fully captured
    • Structural comparison with ENSA-bound state absent
  13. 2025 High

    Identified an additional Cdk1-dependent S23 phosphorylation, removed by Fcp1, that tunes mitotic exit timing and chromosome segregation fidelity.

    Evidence Phospho-specific antibodies, CRISPR endogenous phospho-mutant substitution, okadaic-acid-resistant phosphatase assays, and segregation/timing readouts in human cells

    PMID:40447768

    Open questions at the time
    • How S23 phosphorylation alters PP2A inhibition mechanistically unclear
    • Kinase identity beyond Cdk1-dependence not defined
  14. 2025 Medium

    Connected splicing regulation to ARPP19 output, showing SF3B1 K700E favors exon-2 inclusion to produce an ARPP19-long isoform that sustains PP2A-B55 inhibition and accelerates mitotic exit.

    Evidence RNA-seq and SF3B1 knockdown, ectopic ARPP19-long expression with mitotic timing, and DYRK1A/phosphatase inhibition (preprint)

    PMID:bio_10.1101_2025.05.08.652831

    Open questions at the time
    • Preprint; isoform mechanism not independently confirmed
    • Physiological relevance in SF3B1-mutant disease not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ARPP19's distinct functional modes—mitotic PP2A inhibition, neuronal cAMP switching, and RNA-stability control—are coordinated within a single cell, and what distinguishes ARPP19 from ENSA at the molecular level, remains unresolved.
  • No unified model reconciling cell-cycle and neuronal roles
  • Structural/sequence basis of ARPP19 vs ENSA divergence undefined
  • RNA-binding mechanism uncharacterized at residue level

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 5 GO:0140313 molecular sequestering activity 2 GO:0003723 RNA binding 1
Pathway
R-HSA-1640170 Cell Cycle 4 R-HSA-162582 Signal Transduction 3 R-HSA-1474165 Reproduction 2
Partners
FCP1GAP-43MAST3MASTLPP2APPP2R1APPP2R2DPRKACA

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2010 ARPP19, when phosphorylated by Greatwall kinase, associates with and inhibits PP2A, promoting mitotic entry. In Xenopus egg extracts, endogenous ARPP19 (but not α-Endosulfine/ENSA) is responsible for PP2A inhibition at mitotic entry. Without Greatwall activity, ARPP19 is dephosphorylated and loses its capacity to bind and inhibit PP2A. Biochemical identification of Greatwall substrates in Xenopus egg extracts; co-immunoprecipitation; phosphatase activity assays; depletion/add-back experiments Science High 21164014
2013 Phosphorylation of ARPP19 at S67 by Greatwall kinase promotes its binding to PP2A-B55δ, inhibiting PP2A activity. This process is controlled by Cdk1 and plays an essential role within the Cdk1 auto-amplification loop for entry into the first meiotic division. Once phosphorylated by Greatwall at S67, ARPP19 escapes negative regulation by PKA. Xenopus oocyte microinjection; phospho-specific mutants; PP2A activity assays; co-immunoprecipitation Journal of cell science High 23781026
2014 ARPP19 phosphorylation at serine 109 by PKA is necessary and sufficient for maintaining Xenopus oocytes arrested in prophase. Progesterone promotes partial dephosphorylation of ARPP19 at S109, enabling a threshold level of active Cdk1 to form. Active Cdk1 then initiates the MPF auto-amplification loop requiring Greatwall-dependent phosphorylation of ARPP19 at S67. Thus ARPP19 integrates opposing PKA and Greatwall signals at a crossroads in meiotic M-phase control. Xenopus oocyte microinjection; phospho-specific mutants (S109A, S109D); kinase activity assays; PKA manipulation Nature communications High 24525567
2017 ARPP-16 (the striatum-enriched splice variant sharing the ARPP19 locus) is phosphorylated at Ser46 by MAST3 kinase in vitro and in vivo. This phosphorylation converts ARPP-16 into a selective inhibitor of B55α- and B56δ-containing PP2A heterotrimers. ARPP-16 interacts directly with the PP2A scaffolding A subunit. PKA phosphorylation at Ser88 opposes MAST3, causing dephosphorylation of Ser46 and disinhibition of PP2A. Conditional knockout of ARPP-16 results in dephosphorylation of PP2A substrates including phospho-Thr75-DARPP-32, phospho-T308-Akt, and phospho-T202/Y204-ERK. In vitro kinase assay; co-immunoprecipitation; conditional knockout mouse (CaMKIIα::cre/floxed ARPP-16/19); phospho-specific antibodies; PP2A activity assays The Journal of neuroscience High 28167675
2017 PKA phosphorylation and MAST3 phosphorylation of ARPP-16/19 are mutually suppressive: phosphorylation by PKA prevents MAST3 from acting and prevents PP2A inhibition by MAST3-phosphorylated ARPP-16. PKA also phosphorylates MAST3 at multiple sites, inhibiting MAST3 kinase activity. Together these interactions create a switch-like response to cAMP regulating PP2A activity in striatal neurons. In vitro kinase assays; mass spectrometry; mathematical modeling; phospho-mutant analysis eLife High 28613156
2019 Using conditional knockout mouse models, ARPP19 (but not ENSA) was found essential for mouse embryogenesis. Arpp19 ablation dramatically decreased MEF viability by perturbing the temporal pattern of protein dephosphorylation during mitotic progression, consistent with a drop in PP2A-B55 activity inhibition. ENSA could not compensate for ARPP19 loss in mitotic division. By contrast, ENSA ablation (but not ARPP19 ablation) perturbed S phase. Conditional knockout mouse models (Arpp19 and Ensa); mouse embryonic fibroblast viability assays; cell cycle analysis; phospho-protein timing analysis The Journal of cell biology High 30626720
2021 Molecular determinants of ARPP19's S67 phosphorylation confer high affinity and slow dephosphorylation kinetics when bound to PP2A-B55, enabling it to act as a competitive inhibitor of PP2A-B55 substrates. Phospho-S109 (PKA site) restricts S67 phosphorylation by increasing PP2A-B55-catalyzed dephosphorylation of S67, and a double feedback loop between S67 and S109 phosphorylation sites coordinates PP2A-B55 inhibition with Cyclin B/Cdk1 activation during cell division. In vitro phosphatase kinetics assays; phospho-mutant analysis; binding affinity measurements; Xenopus egg extract reconstitution Nature communications High 34117214
2021 PP2A-B55δ is the phosphatase responsible for dephosphorylating ARPP19 at S109 (the PKA site) to initiate prophase release in Xenopus oocytes. In prophase, PKA and PP2A-B55δ are simultaneously active. When progesterone reduces PKA activity, PP2A-B55δ dephosphorylates S109, unlocking the prophase block. Thus PP2A-B55δ acts at two distinct ARPP19 sites—opposing PKA (at S109) and being inhibited by Gwl-phosphorylated ARPP19 (at S67). Xenopus oocyte microinjection; phosphatase inhibitor experiments; PP2A-B55δ immunodepletion; phospho-specific assays Nature communications High 33758202
2023 Cryo-EM structures of PP2A:B55 bound to phosphorylated ARPP19 reveal that the intrinsically disordered ARPP19 binds PP2A:B55 using multiple distinct binding sites on the B55 subunit, explaining how both substrates and inhibitors are recruited to PP2A:B55. Complementary NMR spectroscopy confirmed the structural findings. The structures provide a molecular mechanism for PP2A:B55 inhibition by ARPP19. Single-particle cryo-EM; NMR spectroscopy; biophysical/biochemical assays Nature High 38123684
2025 ARPP19 is phosphorylated in a Cdk1-dependent manner at serine 23 (a site absent in mammalian ENSA) in mitotic human cells, and dephosphorylated at S23 during mitotic exit by the phosphatase Fcp1 (resistant to okadaic acid). Substituting endogenous ARPP19 with a S23-phosphorylation-resistant mutant increased chromosome segregation errors and accelerated mitotic exit; a phosphomimetic S23 mutant delayed mitotic exit. This phosphorylation switch grants timely mitotic exit and chromosome stability. Phospho-specific antibodies in human cells; CRISPR/endogenous substitution with phospho-mutants; phosphatase inhibitor experiments (okadaic acid); chromosome segregation assays; mitotic timing assays Communications biology High 40447768
2001 ARPP-16 and ARPP-19 are substrates for PKA; both proteins contain a conserved consensus PKA phosphorylation site (RKPSLVA). In striatal slices, ARPP-16 phosphorylation increases in response to D1 dopamine receptor activation and decreases with D2 dopamine receptor activation. In non-neuronal cells, ARPP-19 is highly phosphorylated in response to PKA activation. In vitro kinase assay; phospho-specific antibody immunoblotting; striatal slice pharmacology Journal of neurochemistry Medium 11279279
1990 ARPP-16 and ARPP-19 were purified to homogeneity and identified as substrates for cAMP-dependent protein kinase (PKA). ARPP-19 contains 16 additional NH2-terminal amino acids compared to ARPP-16; both are encoded by related cDNA clones sharing identical 3'-untranslated sequences, suggesting they arise from alternative transcription/splicing. Protein purification; cDNA cloning and sequencing; in vitro PKA phosphorylation assays The Journal of biological chemistry Medium 2160982
2002 ARPP-19 mediates NGF-dependent regulation of GAP-43 mRNA stability. In an NGF-dependent manner, ARPP-19 binds to the 3' region of GAP-43 mRNA that controls its half-life. Mutation of serine 104 (the PKA phosphorylation site) to alanine or aspartate abolished regulation of GAP-43 mRNA reporter expression in PC12 cells, demonstrating that PKA-dependent phosphorylation of ARPP-19 is required for this post-transcriptional function. RNA-protein binding assay; PC12 cell overexpression; reporter assays with 3'UTR constructs; site-directed mutagenesis Proceedings of the National Academy of Sciences of the United States of America Medium 12221279
2017 Greatwall kinase-dependent phosphorylation of ARPP19 at S67 is dominant over PKA-dependent phosphorylation at S109 in controlling Cdk1 activation. Both PKA and Gwl phosphorylate ARPP19 independently of each other. Cdk1 is not directly involved in regulating the biological activity of ARPP19. Xenopus oocyte microinjection; phospho-specific mutants; kinase activity assays Cell cycle Medium 28722544
2020 In human platelets, ARPP19 S62 is phosphorylated by MASTL (or a related kinase) and both S62 and S104 are dephosphorylated by platelet PP2A. Only S62-phosphorylated ARPP19 (but not S104-phosphorylated) acts as a PP2A inhibitor in this context. The entire MASTL-ENSA/ARPP19-PP2A pathway is present and active in anucleate platelets. Proteomic analysis; recombinant protein phosphorylation assays with MASTL, PKA, PKG; phospho-mutant analysis; PP2A activity assays in platelets Cells Medium 32085646
2021 ARPP-19 and ARPP-16 are intrinsically disordered proteins. Their interaction with PP2A is mediated by a linear motif interacting with the PP2A A subunit (modest affinity), and both proteins transiently interact with the B56 subunit weakly via multiple interaction motifs. NMR spectroscopy; SAXS; microscale thermophoresis Frontiers in molecular biosciences Medium 33842550
2025 SF3B1 K700E mutation increases inclusion of ARPP19 exon 2, producing an ARPP19-long isoform that sustains PP2A-B55 inhibition and promotes mitotic progression. Ectopic expression of ARPP19-long accelerated mitotic exit. Pharmacological inhibition of DYRK1A or broad serine/threonine phosphatases shifted ARPP19 exon 2 inclusion in the same direction as SF3B1 K700E, indicating a kinase-phosphatase signaling axis influences this splice event. RNA-seq in K562 cells expressing SF3B1 K700E; siRNA knockdown of SF3B1 in HeLa cells; ectopic ARPP19-long overexpression; mitotic timing assays; pharmacological inhibition bioRxivpreprint Medium bio_10.1101_2025.05.08.652831

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A. Science (New York, N.Y.) 354 21164014
2015 MicroRNA-320a sensitizes tamoxifen-resistant breast cancer cells to tamoxifen by targeting ARPP-19 and ERRγ. Scientific reports 80 25736597
1990 Differential expression of ARPP-16 and ARPP-19, two highly related cAMP-regulated phosphoproteins, one of which is specifically associated with dopamine-innervated brain regions. The Journal of neuroscience : the official journal of the Society for Neuroscience 57 2158525
1994 Expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human brain tissue. The Journal of neuroscience : the official journal of the Society for Neuroscience 53 8120638
2002 Nerve growth factor controls GAP-43 mRNA stability via the phosphoprotein ARPP-19. Proceedings of the National Academy of Sciences of the United States of America 50 12221279
2001 ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins. Journal of neurochemistry 47 11279279
1990 Purification and cDNA cloning of ARPP-16, a cAMP-regulated phosphoprotein enriched in basal ganglia, and of a related phosphoprotein, ARPP-19. The Journal of biological chemistry 46 2160982
2001 Decreased levels of ARPP-19 and PKA in brains of Down syndrome and Alzheimer's disease. Journal of neural transmission. Supplementum 45 11771749
2014 Phosphorylation of ARPP19 by protein kinase A prevents meiosis resumption in Xenopus oocytes. Nature communications 43 24525567
2012 MicroRNA-320 induces neurite outgrowth by targeting ARPP-19. Neuroreport 38 22617447
2019 ENSA and ARPP19 differentially control cell cycle progression and development. The Journal of cell biology 36 30626720
2020 LncRNA IGFL2-AS1 functions as a ceRNA in regulating ARPP19 through competitive binding to miR-802 in gastric cancer. Molecular carcinogenesis 33 31943339
2017 ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase). The Journal of neuroscience : the official journal of the Society for Neuroscience 33 28167675
2023 Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. Nature 32 38123684
2020 Long Noncoding RNA DLX6-AS1 Promotes the Progression in Cervical Cancer by Targeting miR-16-5p/ARPP19 Axis. Cancer biotherapy & radiopharmaceuticals 32 32077747
2020 The Cell Cycle Checkpoint System MAST(L)-ENSA/ARPP19-PP2A is Targeted by cAMP/PKA and cGMP/PKG in Anucleate Human Platelets. Cells 23 32085646
2017 Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. eLife 23 28613156
2013 The phosphorylation of ARPP19 by Greatwall renders the auto-amplification of MPF independently of PKA in Xenopus oocytes. Journal of cell science 23 23781026
2016 ARPP-19 promotes proliferation and metastasis of human glioma. Neuroreport 22 27380244
2018 MiR-26a inhibits thyroid cancer cell proliferation by targeting ARPP19. American journal of cancer research 21 30034940
2014 Increased ARPP-19 expression is associated with hepatocellular carcinoma. International journal of molecular sciences 17 25547487
2015 The mitotic PP2A regulator ENSA/ARPP-19 is remarkably conserved across plants and most eukaryotes. Biochemical and biophysical research communications 14 25666948
2011 Greatwall kinase, ARPP-19 and protein phosphatase 2A: shifting the mitosis paradigm. Results and problems in cell differentiation 13 21630148
2019 Arpp19 Promotes Myc and Cip2a Expression and Associates with Patient Relapse in Acute Myeloid Leukemia. Cancers 12 31717978
2021 The study of the determinants controlling Arpp19 phosphatase-inhibitory activity reveals an Arpp19/PP2A-B55 feedback loop. Nature communications 11 34117214
2021 Long non-coding RNA MCM3AP-AS1 facilitates colorectal cancer progression by regulating the microRNA-599/ARPP19 axis. Oncology letters 9 33613714
2021 The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division. Nature communications 9 33758202
2017 The greatwall kinase is dominant over PKA in controlling the antagonistic function of ARPP19 in Xenopus oocytes. Cell cycle (Georgetown, Tex.) 8 28722544
2000 ARPP-16 mRNA is up-regulated in the longissimus muscle of pigs possessing an elevated growth rate. Journal of animal science 8 10875629
2021 The Interaction Mechanism of Intrinsically Disordered PP2A Inhibitor Proteins ARPP-16 and ARPP-19 With PP2A. Frontiers in molecular biosciences 7 33842550
2021 LncRNA SNHG6 accelerates nasopharyngeal carcinoma progression via modulating miR-26a-5p/ARPP19 axis. Bioorganic & medicinal chemistry letters 6 33744438
2020 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). Biomolecular NMR assignments 6 32468417
2020 cAMP-regulated phosphoproteins DARPP-32, ARPP16/19, and RCS modulate striatal signal transduction through protein kinases and phosphatases. Advances in pharmacology (San Diego, Calif.) 4 33706938
2020 ARPP-19 Mediates Herceptin Resistance via Regulation of CD44 in Gastric Cancer. OncoTargets and therapy 2 32753897
2003 Expression of ARPP-16/19 in rat denervated skeletal muscle. Journal of biochemistry 2 12944371
2025 Proteomic hub proteins CDKN2B, TRAPPC2L, WFS1, and ARPP19 drive biochemical recurrence and metastatic progression in prostate cancer: Protein macromolecule action. International journal of biological macromolecules 0 40345286
2025 Unveiling an Arpp-19 phosphorylation switch that grants chromosome stability. Communications biology 0 40447768
2023 Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. bioRxiv : the preprint server for biology 0 37693408

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