Affinage

ANKRD2

Ankyrin repeat domain-containing protein 2 · UniProt Q9GZV1

Length
360 aa
Mass
39.9 kDa
Annotated
2026-06-09
61 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ANKRD2 (Arpp) is a stretch-responsive, dual-compartment muscle protein of the MARP family that couples mechanical and oxidative stress at the sarcomere to transcriptional programs in the nucleus (PMID:10873377, PMID:17926058). Within striated muscle it localizes to the sarcomeric I-band, where its ankyrin-repeat region binds the elastic protein titin (N2A region) and assembles a mechanosensory complex with myopalladin and the protease calpain-3/p94 (PMID:14583192), and it additionally binds the Z-disc protein telethonin and the PDZ-LIM protein ZASP (PMID:15136035, PMID:24647531). Its expression is induced by passive stretch and denervation and is governed by MyoD, marking ANKRD2 as a downstream effector of the myogenic differentiation program (PMID:10873377, PMID:15890200). Upon muscle injury or oxidative stress, ANKRD2 translocates to the nucleus and partitions to transcriptionally active euchromatin (PMID:17926058); this relocation is gated by Akt2-specific phosphorylation at Ser-99 and is facilitated by complex formation with lamin A, with Ser-99 phosphorylation acting as a negative regulator of myogenic differentiation under stress (PMID:21737686, PMID:28531892). In the nucleus ANKRD2 functions as a transcriptional modulator, binding p53 to enhance activation of the p21 promoter and partnering with ZASP to promote p53 poly-SUMOylation (PMID:15136035, PMID:24647531), while also acting as a repressor of NF-κB inflammatory signaling through phosphorylation-dependent recruitment of the p50 subunit, with Gsk3β identified as a direct target of the p50/ANKRD2 repressosome (PMID:24434510). Genetic ablation of all three MARP proteins yields viable mice with normal cardiac function at baseline and under pressure overload, indicating functional redundancy within the family (PMID:24736439). ANKRD2 mutant-lamin A interactions link it to Emery-Dreifuss muscular dystrophy 2 (EDMD2)-associated lamin A, which aberrantly sequesters ANKRD2 in the nucleus and sensitizes cells to oxidative stress (PMID:28531892).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 2000 Medium

    Identifying ANKRD2 as a transcript induced by passive muscle stretch established it as a mechanically responsive gene and predicted nuclear and signaling features from its sequence.

    Evidence Suppression subtractive hybridization of stretched vs. control mouse skeletal muscle with Northern blot and ORF sequence analysis

    PMID:10873377

    Open questions at the time
    • Functional domains (NLS, PEST, nucleotide-binding) assigned by sequence only, not biochemically validated
    • No protein partners identified at this stage
  2. 2002 Medium

    Demonstrating dual nuclear and I-band localization that shifts with denervation framed ANKRD2 as a candidate signaling shuttle rather than a purely structural sarcomeric protein.

    Evidence Immunohistochemistry across mouse tissues and Western blotting of denervated muscle over time

    PMID:12004005

    Open questions at the time
    • Trigger and machinery for nuclear partitioning unknown
    • Tissue-specific distribution mechanism unexplained
  3. 2003 High

    Placing ANKRD2 in a titin-N2A/myopalladin/calpain-3 complex at the I-band defined its sarcomeric anchoring and implicated it in a mechanosensory signaling module.

    Evidence Ultrastructural immunostaining, co-localization, and co-immunoprecipitation in cardiac myocytes

    PMID:14583192

    Open questions at the time
    • How mechanical signals are transduced from the complex to ANKRD2 release/translocation not resolved
    • Stoichiometry and direct vs. indirect binding within the complex unclear
  4. 2004 High

    Showing direct binding to YB-1, PML, telethonin, and p53 with enhancement of p53-driven p21 promoter activity established ANKRD2 as a transcriptional co-regulator, not just a structural protein.

    Evidence GST pulldown, co-immunoprecipitation, confocal immunofluorescence, and p21 luciferase reporter assay in human myoblasts

    PMID:15136035

    Open questions at the time
    • Whether p53 co-activation occurs in vivo in stressed muscle not shown
    • Functional consequence of YB-1 and PML binding not defined
  5. 2005 Medium

    Connecting ANKRD2 to MyoD control and to the slow-fiber phenotype clarified its regulation and tied its mechanosensing to fiber-type identity rather than hypertrophy.

    Evidence MyoD-silenced C2C12 clones with promoter reporter assays; in vivo stretch/denervation models with RT-PCR, Western blot, and SELDI-TOF proteomics

    PMID:15677738 PMID:15890200

    Open questions at the time
    • Direct MyoD binding to the endogenous promoter vs. indirect effect not fully separated
    • Causal role in fiber-type switching vs. correlation unresolved
  6. 2008 Medium

    Perturbation experiments linked ANKRD2 dosage to the coordination of proliferation and apoptosis during myogenesis, primarily through the p53 network.

    Evidence Stable overexpression and siRNA silencing in C2C12 cells with transcriptional profiling and morpho-physiological analysis

    PMID:18302940

    Open questions at the time
    • p53 pathway link inferred from expression data rather than direct mechanism
    • In vivo relevance not tested
  7. 2007 Medium

    Demonstrating injury-induced translocation to euchromatin in damaged myofibers provided spatial evidence that ANKRD2 acts on transcriptionally active chromatin after mechanical damage.

    Evidence Immunohistochemistry and double-label immunofluorescence on cardiotoxin- and freeze-injured muscle

    PMID:17926058

    Open questions at the time
    • Target genes engaged on euchromatin not identified
    • Signal triggering translocation not defined biochemically
  8. 2011 High

    Identifying Akt2-specific Ser-99 phosphorylation under oxidative stress provided the molecular switch regulating ANKRD2 and its role as a brake on myogenic differentiation.

    Evidence Anti-phospho-Akt substrate proteomics, in vitro kinase assays with recombinant Akt1/Akt2, isoform-specific siRNA, and Ser99Ala mutant differentiation assays in C2C12

    PMID:21737686

    Open questions at the time
    • How Ser-99 phosphorylation mechanistically alters localization or partner binding not directly shown here
    • Upstream activator of Akt2 in this context unresolved
  9. 2011 Medium

    Genome-scale silencing placed ANKRD2 in a regulatory feedback loop with multiple signaling pathways and identified transcription factors that bind both its protein and promoter.

    Evidence Microarray profiling of Ankrd2-silenced human myotubes, promoter binding assays, Co-IP, and reporter assays

    PMID:22016770

    Open questions at the time
    • Breadth of claimed pathway and partner involvement exceeds direct mechanistic validation
    • Which interactions are direct vs. indirect not fully delineated
  10. 2014 High

    Defining the phosphorylation-dependent ANKRD2/p50 repressosome and the ZASP-facilitated p53 SUMOylation complex established two concrete nuclear mechanisms downstream of stress signaling.

    Evidence Genome-wide profiling and Co-IP in Ankrd2-KO/overexpressing myocytes (p50/Gsk3β); yeast two-hybrid, GST pulldown, Co-IP, SUMO assay, and mutagenesis (ZASP/p53)

    PMID:24434510 PMID:24647531

    Open questions at the time
    • In vivo demonstration of NF-κB repression in muscle physiology limited
    • How ZASP competition with p53 is regulated dynamically unclear
  11. 2014 High

    Triple MARP knockout mice showed the family is dispensable for cardiac development and pressure-overload response, establishing functional redundancy and constraining the in vivo essentiality of ANKRD2.

    Evidence Single/double/triple MARP KO mice with echocardiography and hemodynamics at baseline and after transverse aortic constriction

    PMID:24736439

    Open questions at the time
    • Skeletal muscle and stress-specific phenotypes not exhaustively examined
    • Redundant compensatory mechanisms not identified
  12. 2016 Medium

    Resolving four ANKRD2 isoforms with distinct localizations clarified which forms account for sarcomeric versus nuclear functions.

    Evidence Isoform-specific Western blotting, immunohistochemistry, immunofluorescence, and RNAseq in striated muscle and primary myoblasts

    PMID:27393496

    Open questions at the time
    • Functional differences among isoforms beyond localization not characterized
    • Regulation of isoform choice unknown
  13. 2017 Medium

    Showing that EDMD2 mutant lamin A binds and aberrantly sequesters ANKRD2 linked its nuclear shuttling to a laminopathy and to oxidative stress sensitivity.

    Evidence Co-IP, subcellular fractionation, immunofluorescence, ROS measurement, and viability assays in EDMD2 lamin A cell lines and patient myotubes

    PMID:28531892

    Open questions at the time
    • Whether ANKRD2 mislocalization causally contributes to EDMD2 pathology in vivo not established
    • Lamin A binding interface on ANKRD2 not mapped
  14. 2025 Medium

    ANKRD2 knockdown in osteosarcoma cells coupled it to PI3K/Akt and ERK signaling, cell-cycle cyclins, lamin expression, and chemosensitivity, extending its role beyond muscle.

    Evidence siRNA/shRNA knockdown in U2OS and HOS cells with Western blot pathway readouts and drug-response assays

    PMID:40004199

    Open questions at the time
    • Direct molecular targets in the proliferation/lamin axis not identified
    • In vivo tumor relevance not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ANKRD2 mechanically senses sarcomeric strain and integrates Akt2 phosphorylation, lamin A binding, and isoform identity into selective transcription-factor engagement remains unresolved.
  • No structural model of ANKRD2-titin or ANKRD2-transcription factor complexes
  • Causal chain from I-band release to specific gene programs in vivo not established
  • Physiological loss-of-function phenotype in skeletal muscle under stress not fully defined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 3 GO:0008092 cytoskeletal protein binding 2 GO:0098772 molecular function regulator activity 2 GO:0140299 molecular sensor activity 2
Localization
GO:0005634 nucleus 3 GO:0005856 cytoskeleton 2 GO:0000228 nuclear chromosome 1
Pathway
R-HSA-1266738 Developmental Biology 3 R-HSA-162582 Signal Transduction 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-8953897 Cellular responses to stimuli 3
Partners
CAPN3LDB3LMNAMYPNPMLTP53TTNYBX1
Complex memberships
ANKRD2-ZASP-p53 complexp50/ANKRD2 NF-κB repressosometitin N2A-myopalladin-calpain-3 I-band complex

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 ANKRD2/Arpp contains within its ankyrin repeat region a binding site for the myofibrillar elastic protein titin (N2A region), and together with myopalladin and calpain protease p94 forms a titin N2A-based signaling complex at the I-band of striated muscle. Co-localization by ultrastructural immunostaining; complex membership established by co-immunoprecipitation and localization studies in cardiac myocytes Journal of molecular biology High 14583192
2004 ANKRD2 binds the Z-disc protein telethonin, the transcription factor YB-1 (both in vitro and in vivo), the nuclear body protein PML (co-localizes in nuclear bodies by confocal immunofluorescence in human myoblasts), and the tumor suppressor p53 (in vitro and in vivo). ANKRD2 binding to p53 enhances p53-mediated up-regulation of the p21(WAF1/CIP1) promoter. GST pulldown (in vitro binding), co-immunoprecipitation (in vivo), confocal immunofluorescence, luciferase reporter assay for p21 promoter activation Journal of molecular biology High 15136035
2000 Ankrd2 is a stretch-responsive skeletal muscle gene; its transcript exhibits a fourfold increase in expression after 7 days of passive stretch of mouse skeletal muscles in vivo. The encoded protein contains an ATP/GTP binding domain, a nuclear localization signal, two PEST destabilization motifs, and a 132-amino-acid ankyrin-repeat region. Suppression subtractive hybridization of mechanically stretched vs. control mouse skeletal muscle; Northern blot quantification; sequence analysis of open reading frame Genomics Medium 10873377
2002 Arpp/Ankrd2 protein is localized in both the nucleus and the sarcomeric I-band of muscle fibers, and its intracellular distribution is tissue- and context-specific (cytoplasm+nucleus in neurons, nucleus only in pancreas and esophagus). Expression is markedly upregulated in skeletal muscle after denervation and is sustained longer than CARP upregulation. Immunohistochemistry on mouse tissues; Western blotting on denervated muscle at multiple time points Laboratory investigation Medium 12004005
2007 After muscle injury (cardiotoxin injection or dry-ice contact), Arpp/Ankrd2 translocates from the I-band to the nuclei of adjacent sarcomere-damaged myofibers, where it preferentially localizes to euchromatin regions associated with transcriptionally active genes. Immunohistochemistry and double-label immunofluorescence on injured gastrocnemius muscle sections Histochemistry and cell biology Medium 17926058
2011 Akt2 phosphorylates ANKRD2 specifically at Ser-99 in response to oxidative stress (H2O2). This is Akt isoform-specific (Akt2, not Akt1), as demonstrated by in vitro kinase assays with recombinant Akt1 and Akt2 and by single-isoform siRNA silencing. Expression of a phosphorylation-defective Ser-99-Ala mutant of Ankrd2 in C2C12 myoblasts promotes faster myogenic differentiation, placing Akt2-mediated phosphorylation as a negative regulator of myogenesis under stress. Proteomic substrate search with anti-phospho-Akt substrate antibody; in vitro kinase assay with recombinant Akt1 and Akt2; isoform-specific siRNA silencing; overexpression of phosphorylation-defective mutant in C2C12 cells with differentiation assay Molecular biology of the cell High 21737686
2014 ANKRD2 acts as a potent repressor of NF-κB-mediated inflammatory responses through direct interaction with the NF-κB repressor subunit p50. Recruitment of p50 by Ankrd2 is dependent on Akt2-mediated phosphorylation of Ankrd2 upon oxidative stress. Gsk3β was identified as a novel direct target gene of the p50/Ankrd2 repressosome. In slow muscle, absence of Ankrd2 negatively affects expression of cytokines and calcineurin-dependent genes associated with the slow-twitch muscle program. Genome-wide expression profiling of Ankrd2-KO and -overexpressing myoblasts/myotubes; co-immunoprecipitation of Ankrd2 with p50; loss-of-function (KO) phenotypic analysis in primary muscle cells Cell death & disease High 24434510
2014 ZASP (a PDZ-LIM protein) interacts directly with Ankrd2 and p53, forming a triple complex that facilitates poly-SUMOylation of p53. The ZASP PDZ domain binds both Ankrd2 and p53 at non-competing sites. The ZASP ZM-motif region competes with p53 for the same binding site on Ankrd2. The zaspopathy-causing mutation A165V in ZASP abolishes its ability to bind Ankrd2. Co-immunoprecipitation, GST pulldown, yeast two-hybrid, SUMO modification assay, luciferase reporter assay, mutagenesis PloS one High 24647531
2011 Silencing Ankrd2 in human myotubes alters expression of genes involved in multiple signaling pathways (MAPK, p53, TGF-β, Wnt, calcium, insulin signaling, cytoskeleton regulation). Novel upstream effectors Nkx2.5 and p53 were identified for the Ankrd2 gene promoter. Ankrd1/CARP was shown to modulate MyoD transcriptional activity on the Ankrd2 promoter. Ankrd2 also interacts with proteins containing PDZ and SH3 domains. Transcription factors PAX6, LHX2, NFIL3, and MECP2 bind both the Ankrd2 protein and its promoter, indicating a regulatory feedback loop. Expression profiling of Ankrd2-silenced human myotubes (microarray); promoter binding assays; co-immunoprecipitation for PDZ/SH3 domain interactions; reporter assays for Ankrd2 promoter PloS one Medium 22016770
2005 Ankrd2 expression in fast tibialis anterior muscle is upregulated by passive stretch but is associated with the slow-muscle phenotype shift rather than hypertrophy per se. In kyphoscoliotic mutant mice (which adopt a slower fiber phenotype without hypertrophy), Ankrd2 is upregulated. Denervation of rat soleus (which shifts to fast phenotype) markedly downregulates Ankrd2 protein (undetectable by SELDI-TOF proteomics after 4 weeks). Ankrd2 is a titin-binding protein. In vivo stretch immobilization; RT-PCR and Western blot for Ankrd2 mRNA and protein; SELDI-TOF proteomics on denervated soleus; genetic mouse model (kyphoscoliotic mutant) Journal of applied physiology Medium 15677738
2005 Ankrd2 transcription is under the control of MyoD during myogenic differentiation. Silencing MyoD in C2C12 cells alters Ankrd2 expression, and bioinformatic and functional promoter studies confirm Ankrd2 as a downstream MyoD target gene. C2C12 MyoD-silenced clones; muscle-specific cDNA microarray; promoter functional analysis (reporter assays) Journal of molecular biology Medium 15890200
2008 Overexpression or silencing of Ankrd2 in C2C12 myocytes perturbs coordination of proliferation and apoptosis during myogenic differentiation in vitro, mainly through the p53 network, as revealed by transcriptional profiling and morpho-physiological analysis. Stable overexpression and siRNA silencing in C2C12 cells; transcriptional profiling; morphological and biochemical analysis of differentiation Biochimica et biophysica acta Medium 18302940
2017 EDMD2-associated mutant forms of lamin A bind Ankrd2 (co-immunoprecipitation) and aberrantly sequester/mislocalize Ankrd2 in the nucleus even under basal conditions. Oxidative stress normally induces formation of an Ankrd2–lamin A complex and nuclear translocation of Ankrd2; EDMD2 mutations constitutively mimic this state. Cells co-expressing Ankrd2 and EDMD2 lamin A mutants show increased sensitivity to oxidative stress. Co-immunoprecipitation, cellular subfractionation, immunofluorescence in EDMD2-lamin A overexpressing cell lines and patient myotubes; ROS measurement and cell viability assays Cellular physiology and biochemistry Medium 28531892
2014 MARP triple knockout mice (lacking CARP, Ankrd2, and DARP) are viable and have normal cardiac function at baseline and after transverse aortic constriction (pressure overload), demonstrating that the three MARP proteins are not individually or collectively essential for normal cardiac development or the response to mechanical pressure overload. Generation of single, double, and triple MARP KO mice; echocardiography and hemodynamic studies at baseline and after TAC PloS one High 24736439
2025 Ankrd2 knockdown in osteosarcoma cells (U2OS, HOS) impairs activation of PI3K/Akt and ERK1/2 pathways, reduces cyclin D1 and cyclin B levels, disrupts nuclear lamin A and lamin B expression, and enhances sensitivity to doxorubicin and cisplatin. siRNA/shRNA knockdown in osteosarcoma cell lines; Western blotting for pathway components; cell viability and drug response assays International journal of molecular sciences Medium 40004199
2020 ANKRD2 is a target of miR-205-5p and plays an essential role in modulating NF-κB signaling in head and neck squamous cell carcinoma cells, as demonstrated by RNA-seq and experimental validation downstream of the lncRNA VENTXP1/miR-205-5p axis. RNA-seq differential expression analysis; miR-205-5p target validation (luciferase reporter and Western blot); ANKRD2 KD with NF-κB pathway readout Cell death & disease Medium 33037177
2025 Ankrd2 overexpression in a denervation-induced muscle atrophy model significantly alleviates muscle atrophy and is associated with downregulation of NF-κB signaling and suppression of pro-atrophy genes in the ubiquitin-proteasome and autophagic-lysosomal systems. Lentivirus-mediated Ankrd2 overexpression in tibialis anterior; transcriptome sequencing (RNA-seq); GO/KEGG pathway analysis; RT-qPCR validation Turkish journal of biology Low 42058127
2016 Four human ANKRD2 protein isoforms (360, 333, 327, and 300 aa) are differentially expressed in striated muscle. The 333 aa isoform is dominant in both skeletal and cardiac muscle and accounts for known sarcomeric/I-band and intercalated disk localizations. The 360 aa isoform has distinct nuclear localization in skeletal muscle and primary myoblasts/myotubes and is not preferentially expressed in slow fibers. Western blotting with isoform-specific antibodies; immunohistochemistry; immunofluorescence in primary myoblasts/myotubes; RNAseq Histochemistry and cell biology Medium 27393496

Source papers

Stage 0 corpus · 61 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules. Journal of molecular biology 289 14583192
1999 Expression of the striatal DARPP-32/ARPP-21 phenotype in GABAergic neurons requires neurotrophins in vivo and in vitro. The Journal of neuroscience : the official journal of the Society for Neuroscience 126 10377350
2004 The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle. Journal of molecular biology 116 15136035
2000 Identification of Ankrd2, a novel skeletal muscle gene coding for a stretch-responsive ankyrin-repeat protein. Genomics 101 10873377
2015 MicroRNA-320a sensitizes tamoxifen-resistant breast cancer cells to tamoxifen by targeting ARPP-19 and ERRγ. Scientific reports 80 25736597
2002 Arpp, a new homolog of carp, is preferentially expressed in type 1 skeletal muscle fibers and is markedly induced by denervation. Laboratory investigation; a journal of technical methods and pathology 68 12004005
2002 Carp, a cardiac ankyrin-repeated protein, and its new homologue, Arpp, are differentially expressed in heart, skeletal muscle, and rhabdomyosarcomas. The American journal of pathology 65 12000728
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
2014 The muscle ankyrin repeat proteins CARP, Ankrd2, and DARP are not essential for normal cardiac development and function at basal conditions and in response to pressure overload. PloS one 51 24736439
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
2011 Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2)O(2). Molecular biology of the cell 48 21737686
2001 ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated phosphoproteins. Journal of neurochemistry 47 11279279
2001 Characterization of human skeletal muscle Ankrd2. Biochemical and biophysical research communications 46 11444853
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
2012 MicroRNA-320 induces neurite outgrowth by targeting ARPP-19. Neuroreport 38 22617447
2014 Ankrd2 is a modulator of NF-κB-mediated inflammatory responses during muscle differentiation. Cell death & disease 36 24434510
2005 Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function. Journal of applied physiology (Bethesda, Md. : 1985) 34 15677738
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
2007 Arpp/Ankrd2, a member of the muscle ankyrin repeat proteins (MARPs), translocates from the I-band to the nucleus after muscle injury. Histochemistry and cell biology 33 17926058
2011 Multi-tasking role of the mechanosensing protein Ankrd2 in the signaling network of striated muscle. PloS one 32 22016770
2008 The effects of Ankrd2 alteration indicate its involvement in cell cycle regulation during muscle differentiation. Biochimica et biophysica acta 32 18302940
2019 Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies. Oxidative medicine and cellular longevity 27 31428229
2014 ZASP interacts with the mechanosensing protein Ankrd2 and p53 in the signalling network of striated muscle. PloS one 27 24647531
2005 The Ankrd2, Cdkn1c and calcyclin genes are under the control of MyoD during myogenic differentiation. Journal of molecular biology 26 15890200
2000 Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in the basal ganglia. Neuropharmacology 26 10854908
2017 Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. eLife 23 28613156
1989 ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions. I. Purification and characterization of the protein from bovine caudate nucleus. The Journal of neuroscience : the official journal of the Society for Neuroscience 23 2538584
1989 ARPP-21, a cyclic AMP-regulated phosphoprotein (Mr = 21,000) enriched in dopamine-innervated brain regions. Amino acid sequence of the site phosphorylated by cyclic AMP in intact cells and kinetic studies of its phosphorylation in vitro. The Journal of biological chemistry 23 2540203
2020 Epigenetic regulation of VENTXP1 suppresses tumor proliferation via miR-205-5p/ANKRD2/NF-kB signaling in head and neck squamous cell carcinoma. Cell death & disease 22 33037177
2016 ARPP-19 promotes proliferation and metastasis of human glioma. Neuroreport 22 27380244
1990 ARPP-21, a cAMP-regulated phosphoprotein enriched in dopamine-innervated brain regions: tissue distribution and regulation of phosphorylation in rat brain. Neuroscience 22 1966823
2017 Emery-Dreifuss Muscular Dystrophy-Associated Mutant Forms of Lamin A Recruit the Stress Responsive Protein Ankrd2 into the Nucleus, Affecting the Cellular Response to Oxidative Stress. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 18 28531892
2004 Altered expression of ARPP protein in skeletal muscles of patients with muscular dystrophy, congenital myopathy and spinal muscular atrophy. Pathobiology : journal of immunopathology, molecular and cellular biology 18 14555844
2014 Increased ARPP-19 expression is associated with hepatocellular carcinoma. International journal of molecular sciences 17 25547487
2007 ARPP protein is selectively expressed in renal oncocytoma, but rarely in renal cell carcinomas. Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc 17 17206105
2015 Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes. Histochemistry and cell biology 16 25585647
2015 The mitotic PP2A regulator ENSA/ARPP-19 is remarkably conserved across plants and most eukaryotes. Biochemical and biophysical research communications 14 25666948
2012 Early depression of Ankrd2 and Csrp3 mRNAs in the polyribosomal and whole tissue fractions in skeletal muscle with decreased voluntary running. Journal of applied physiology (Bethesda, Md. : 1985) 14 22282489
1993 Dopamine D1 agonist SKF 38393 increases the state of phosphorylation of ARPP-21 in substantia nigra. Journal of neurochemistry 14 8436957
2011 Greatwall kinase, ARPP-19 and protein phosphatase 2A: shifting the mitosis paradigm. Results and problems in cell differentiation 13 21630148
2021 Ectopic Expression of Ankrd2 Affects Proliferation, Motility and Clonogenic Potential of Human Osteosarcoma Cells. Cancers 11 33419058
1991 Characterization of rat ARPP-21 mRNA: sequence analysis, tissue distribution, and regulation. Journal of neurochemistry 11 1940913
1989 Localization of ARPP-90, a major 90 kiloDalton basal ganglion-enriched substrate for cyclic AMP-dependent protein kinase, in striatonigral neurons in the rat brain. Brain research. Molecular brain research 10 2541303
1989 ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Molecular cloning and nucleotide sequence. The Journal of neuroscience : the official journal of the Society for Neuroscience 10 2552037
1989 ARPP-21, a cyclic AMP-regulated phosphoprotein enriched in dopamine-innervated brain regions. I. Amino acid sequence of ARPP-21B from bovine caudate nucleus. The Journal of neuroscience : the official journal of the Society for Neuroscience 9 2552036
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
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
2016 Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles. Histochemistry and cell biology 6 27393496
1989 Inhibition of phosphoribosylpyrophosphate synthetase by 4-methoxy-(MRPP) and 4-amino-8-(D-ribofuranosylamino) pyrimido[5,4-d]pyrimidine (ARPP). Biochemical pharmacology 6 2479382
2020 Cloning and expression profiling of muscle regulator ANKRD2 in domestic chicken Gallus gallus. Histochemistry and cell biology 5 32653935
1996 ARPP-21: murine gene structure and promoter identification of a neuronal phosphoprotein enriched in the limbic striatum. Brain research 3 8869551
2020 ARPP-19 Mediates Herceptin Resistance via Regulation of CD44 in Gastric Cancer. OncoTargets and therapy 2 32753897
2017 α-Endosulfine (ARPP-19e) Expression in a Rat Model of Stroke. Journal of neuropathology and experimental neurology 2 28922851
2003 Expression of ARPP-16/19 in rat denervated skeletal muscle. Journal of biochemistry 2 12944371
1993 ARPP-39, a membrane-associated substrate for cyclic AMP-dependent protein kinase present in neostriatal neurons. Journal of molecular neuroscience : MN 2 8217521
2025 ANKRD2 Knockdown as a Therapeutic Strategy in Osteosarcoma: Effects on Proliferation and Drug Response in U2OS and HOS Cells. International journal of molecular sciences 1 40004199
2025 Unveiling an Arpp-19 phosphorylation switch that grants chromosome stability. Communications biology 0 40447768
2025 Ankrd2 may alleviate denervation-induced skeletal muscle atrophy by inhibiting inflammation. Turkish journal of biology = Turk biyoloji dergisi 0 42058127

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