Affinage

PRKRA

Interferon-inducible double-stranded RNA-dependent protein kinase activator A · UniProt O75569

Round 2 corrected
Length
313 aa
Mass
34.4 kDa
Annotated
2026-04-28
130 papers in source corpus 43 papers cited in narrative 43 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PRKRA (PACT/RAX) is a modular double-stranded RNA-binding protein that functions as a context-dependent regulator of PKR kinase activity, innate immune RNA sensors, and microRNA biogenesis. Under basal conditions PACT is held inactive through heterodimerization with TRBP; diverse cellular stresses trigger sequential phosphorylation at Ser246 and Ser287 in PACT's domain 3, promoting TRBP dissociation, PACT homodimerization, high-affinity PKR binding, and disruption of PKR's autoinhibitory intramolecular interaction, culminating in eIF2α phosphorylation, translation inhibition, and apoptosis (PMID:16982605, PMID:21526770, PMID:16785445, PMID:18936160). Independently of PKR, PACT directly stimulates the innate immune sensors RIG-I (by activating its ATPase) and MDA5 (by promoting oligomerization), and is a component of the Dicer–TRBP RISC-loading complex where it modulates miRNA isomiR production (PMID:21501829, PMID:28760879, PMID:16424907, PMID:23661684). Homozygous loss-of-function mutations in PRKRA, notably P222L, cause the autosomal recessive dystonia-parkinsonism disorder DYT16, linked to dysregulated PACT–PKR signaling and an overactive integrated stress response (PMID:18243799, PMID:33049316).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1998 High

    Identification of PACT as the first cellular protein activator of PKR established that PKR can be activated independently of dsRNA, opening the question of how endogenous signals regulate the translational stress response.

    Evidence In vitro kinase reconstitution, co-immunoprecipitation, and yeast co-expression growth inhibition assay

    PMID:9687506

    Open questions at the time
    • Physiological stress signals upstream of PACT unknown
    • Mechanism of activation (direct allosteric vs. scaffolding) unresolved
    • Relationship to other dsRNA-binding proteins not explored
  2. 1999 High

    Demonstrating that the mouse ortholog RAX is rapidly phosphorylated and binds PKR following diverse stresses (IL-3 deprivation, arsenite, peroxide) established PACT/RAX as a general stress-to-translational-inhibition relay upstream of eIF2α.

    Evidence Co-immunoprecipitation after multiple stress treatments, in vitro kinase and eIF2α phosphorylation assays

    PMID:10336432

    Open questions at the time
    • Identity of the kinase phosphorylating RAX unknown
    • Whether different stresses use different phosphosites unresolved
  3. 2001 High

    Domain dissection revealed that PACT's two N-terminal dsRNA-binding domains mediate PKR binding while the C-terminal domain 3 is specifically required for PKR activation, establishing separable binding and activation modules.

    Evidence Systematic domain deletion/fusion mutagenesis with in vitro kinase and cell-based PKR activation assays

    PMID:11238927

    Open questions at the time
    • Structural basis of domain 3 activation function unresolved
    • Whether domain 3 contacts the kinase domain directly not shown
  4. 2006 High

    Identification of Ser246 (constitutive) and Ser287 (stress-induced) phosphorylation in domain 3 as a hierarchical switch for PACT activation, together with NMR evidence that PACT disrupts PKR's autoinhibitory intramolecular interaction, provided the core mechanism of stress-dependent PKR activation.

    Evidence Alanine-scanning mutagenesis, phosphomimetic substitutions, 32P labeling, NMR of PKR intramolecular contacts, decoy peptide assay

    PMID:16785445 PMID:16982605

    Open questions at the time
    • Identity of the kinase(s) phosphorylating Ser246 and Ser287 unknown
    • Full atomic-resolution structure of the PACT–PKR complex lacking
  5. 2006 High

    Discovery that PACT is a stable subunit of the ~500 kDa Dicer–TRBP–Ago2 RISC-loading complex, and that PACT depletion reduces mature miRNA levels, revealed a PKR-independent function in microRNA biogenesis.

    Evidence Reciprocal co-immunoprecipitation, size-exclusion chromatography, siRNA depletion with Northern blot for mature miRNAs

    PMID:16424907

    Open questions at the time
    • Mechanism by which PACT facilitates RISC assembly versus Dicer cleavage not fully dissected
    • In vivo contribution relative to TRBP unclear
  6. 2008 High

    Mapping the DYT16 locus to a homozygous P222L PRKRA mutation in two unrelated families established PACT as the causative gene for autosomal recessive dystonia-parkinsonism, directly linking stress-response signaling to a movement disorder.

    Evidence Autozygosity mapping, candidate gene sequencing, segregation analysis in two independent families; independently replicated in a Polish family

    PMID:18243799 PMID:25142429

    Open questions at the time
    • How P222L alters PACT structure and PKR interaction at atomic level unresolved
    • Cell-type-specific vulnerability in basal ganglia not explained
  7. 2008 High

    Demonstration that TRBP physically sequesters PACT under basal conditions and that stress-induced dissociation of the TRBP–PACT complex licenses PACT to activate PKR identified TRBP as the proximal negative regulator gating PACT's activating function.

    Evidence TRBP-null fibroblasts, siRNA knockdown, co-immunoprecipitation before and after stress, PKR phosphorylation assay

    PMID:18936160

    Open questions at the time
    • Whether TRBP–PACT ratio varies physiologically across tissues not addressed
    • Signaling pathway triggering TRBP–PACT dissociation unclear
  8. 2011 High

    Discovery that PACT directly binds RIG-I's C-terminal repression domain and stimulates RIG-I ATPase activity independently of dsRNA, PKR, or Dicer revealed PACT as a critical co-activator of innate immune RNA sensing beyond its PKR function.

    Evidence Co-immunoprecipitation with domain mapping, ATPase assay, siRNA depletion reducing IFN induction, interferon reporter

    PMID:21501829

    Open questions at the time
    • Structural basis of PACT–RIG-I interaction not determined
    • Whether PACT also activates RIG-I in vivo during specific viral infections not systematically tested
  9. 2011 High

    Showing that Ser287 phosphorylation weakens TRBP–PACT interaction while enhancing PACT homodimerization unified the phosphorylation, TRBP-release, and homodimerization steps into a single coherent activation cascade.

    Evidence Site-directed mutagenesis, co-immunoprecipitation of homo- and heterodimers, PKR activation and apoptosis assays

    PMID:21526770 PMID:22473766

    Open questions at the time
    • Quantitative kinetic parameters for each step not measured
    • Whether additional post-translational modifications contribute unknown
  10. 2013 High

    Reconstitution of Dicer–PACT and Dicer–TRBP complexes showed that PACT and TRBP have non-redundant effects on miRNA isomiR profiles and pre-siRNA processing, with the two N-terminal dsRBDs conferring specificity, refining PACT's role in miRNA-mediated gene regulation.

    Evidence In vitro cleavage assay with purified recombinant proteins, chimeric domain-swap proteins, deep sequencing of isomiRs

    PMID:23661684

    Open questions at the time
    • In vivo contribution of PACT versus TRBP to specific miRNA populations not determined genome-wide
    • Whether PACT affects strand selection during RISC loading unclear
  11. 2013 High

    Demonstrating that EBOV VP35 and HSV-1 Us11 each antagonize PACT's ability to activate RIG-I (and that PACT-knockout cells are insensitive to these viral antagonists) established PACT-mediated innate sensing as a major target of viral immune evasion.

    Evidence PACT-KO MEFs, ATPase assay, co-immunoprecipitation, Us11-deficient virus comparison, IFN production measurement

    PMID:23870315 PMID:24067967

    Open questions at the time
    • How many additional viral proteins target PACT-RIG-I axis unknown
    • Whether PACT directly senses any viral RNA species remains untested
  12. 2015 High

    Genetic epistasis in Rax/Pkr double-knockout mice rescuing pituitary hypoplasia revealed that PACT paradoxically functions as a negative regulator of PKR in pituitary tissue, restraining PKR-dependent growth arrest and enabling postnatal cell proliferation.

    Evidence Double-KO mouse genetics, kinase-dead PKR knock-in rescue, eIF2α(S51A) heterozygous partial rescue, p21 induction in pituitary cell lines

    PMID:26414443

    Open questions at the time
    • Molecular basis of tissue-specific PACT-PKR relationship (activator vs. inhibitor) unknown
    • Whether TRBP levels differ in pituitary not tested
  13. 2015 High

    Demonstrating that PACT promotes MDA5 oligomerization and dsRNA recruitment extended PACT's innate immune co-activator role to the second major cytoplasmic RNA sensor, establishing PACT as a shared cofactor for both RIG-I and MDA5 pathways.

    Evidence PACT-KO cells, interferon reporter, MDA5 oligomerization assay, co-localization by immunofluorescence

    PMID:28760879

    Open questions at the time
    • Stoichiometry and structural basis of PACT–MDA5 filament interaction unresolved
    • Whether PACT distinguishes self vs. non-self RNA in the MDA5 context unknown
  14. 2020 High

    Patient-derived DYT16 lymphoblasts carrying P222L and other mutations showed enhanced PACT–PACT interaction, elevated PKR activation, dysregulated ISR, and increased ER-stress-induced apoptosis — rescued by the PACT–PKR inhibitor luteolin — providing a mechanistic link from mutations to disease pathology and a pharmacological proof-of-concept.

    Evidence Patient lymphoblast ISR analysis, co-immunoprecipitation, kinase assay, luteolin pharmacological rescue, apoptosis assay

    PMID:33049316

    Open questions at the time
    • Whether luteolin is effective in neuronal cells or animal DYT16 models untested
    • Neuronal cell-type-specific consequences of enhanced PACT–PKR signaling not characterized
  15. 2025 High

    A genome-wide CRISPR screen identified PACT as a key inhibitor (not only activator) of PKR during viral infection, and demonstrated that PACT cooperates with ADAR1 to suppress PKR hyperactivation by endogenous self-dsRNAs; simultaneous loss of PACT and ADAR1 causes synthetic lethality fully rescued by PKR deletion.

    Evidence CRISPR-Cas9 genome-wide KO screen (CRISPR-Translate), double-KO cell lines, PKR-KO rescue, translation assay

    PMID:40185749

    Open questions at the time
    • Mechanism by which PACT inhibits rather than activates PKR in the viral/self-RNA context not molecularly defined
    • Whether PACT/ADAR1 cooperativity varies across cell types untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major open questions include: the identity of the kinase(s) phosphorylating PACT at Ser246/Ser287, the structural basis of context-dependent PKR activation versus inhibition, how tissue-specific PACT function is determined (e.g. pituitary versus immune cells), and whether PACT–PKR pathway modulation is therapeutically viable for DYT16 dystonia.
  • Upstream kinase(s) for Ser246/Ser287 not identified
  • No high-resolution structure of the PACT–PKR complex
  • Molecular basis for PACT acting as PKR activator in some contexts and inhibitor in others remains undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 8 GO:0003723 RNA binding 5 GO:0060090 molecular adaptor activity 3
Localization
GO:0005829 cytosol 3
Pathway
R-HSA-168256 Immune System 7 R-HSA-392499 Metabolism of proteins 6 R-HSA-8953897 Cellular responses to stimuli 5 R-HSA-5357801 Programmed Cell Death 4 R-HSA-8953854 Metabolism of RNA 4 R-HSA-1643685 Disease 3
Partners
ADARAGO2DDX58DHX58DICER1EIF2AK2IFIH1TARBP2
Complex memberships
Dicer–TRBP–PACT RISC-loading complexPACT–PKR signaling complexPACT–TRBP heterodimer

Evidence

Reading pass · 43 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 PACT (encoded by PRKRA) was identified as a direct cellular activator of PKR: it heterodimerizes with PKR and activates it in vitro in the absence of dsRNA, and overexpression of PACT in mammalian cells causes PKR activation; co-expression in yeast enhanced PKR's anti-growth effect. In vitro kinase assay, co-immunoprecipitation, yeast co-expression growth assay The EMBO journal High 9687506
1999 RAX (mouse ortholog of PACT/PRKRA) directly activates PKR in vitro; under IL-3 deprivation and diverse stress treatments (arsenite, thapsigargin, H2O2), RAX is rapidly phosphorylated, associates with PKR, and activates it, coupling transmembrane stress signals to protein synthesis inhibition via eIF2α phosphorylation. In vitro kinase assay, co-immunoprecipitation after stress, eIF2α phosphorylation assay The Journal of biological chemistry High 10336432
2001 PACT has a modular structure: domains 1 or 2 are each sufficient for high-affinity binding to PKR, while domain 3 (66 residues) is absolutely required for PKR activation both in vitro and in vivo. Domain 3 fused to a heterologous PKR-binding domain can activate PKR in vivo, demonstrating separable binding and activation functions. Domain deletion/fusion mutagenesis, in vitro kinase assay, cell-based PKR activation assays Molecular and cellular biology High 11238927
2001 Ceramide activates PKR through RAX/PACT: ceramide induces phosphorylation of RAX and eIF2α, and overexpression of RAX potentiates ceramide-induced killing and protein synthesis inhibition; a serine/threonine kinase inhibitor (2-aminopurine) blocks both RAX potentiation and ceramide-induced translation inhibition. Overexpression, eIF2α phosphorylation assay, cell viability assay, kinase inhibitor The Journal of biological chemistry Medium 11148216
2002 HSV-1 Us11 protein inhibits PACT-mediated PKR activation both in vitro and in vivo. Us11 binds both PKR and PACT, but binding to the N-terminal domain of PKR (not to PACT) is essential for inhibition; Us11 does not block PACT-PKR binding but prevents PKR activation. In vitro kinase assay, co-immunoprecipitation, mutational analysis of Us11 Journal of virology High 12368348
2003 TRBP and PACT interact with PKR through the same residues; however, the carboxy-terminal M3 motif of TRBP mediates its inhibitory effect on PKR activity, whereas the corresponding domain of PACT mediates activation, as demonstrated by domain-swap experiments. Domain swap mutagenesis, PKR activity assay, point mutant binding analysis Virology Medium 14585331
2004 RAX (PRKRA mouse ortholog) is phosphorylated on serine 18 following stress. The non-phosphorylatable RAX(S18A) mutant can bind dsRNA and associate with PKR but fails to activate PKR after stress, acting as a dominant negative; stable expression of RAX(S18A) delays translation inhibition and prevents rapid apoptosis after IL-3 withdrawal. Site-directed mutagenesis, kinase assay, dominant-negative expression, eIF2α phosphorylation The Journal of biological chemistry High 15299031
2006 Phosphorylation of two specific serine residues in PACT's domain 3 (Ser246 and Ser287) is essential for PKR activation and apoptosis: Ser246 is constitutively phosphorylated and required for stress-induced phosphorylation of Ser287; substitution of both with phosphomimetic aspartate produces constitutively active PACT that activates PKR even in unstressed cells. Alanine-scanning mutagenesis, 2D gel analysis, phosphoamino acid-specific antisera, 32P labeling, in vivo PKR activation assay The Journal of biological chemistry High 16982605
2006 PKR activation by PACT or dsRNA occurs through disruption of an intramolecular inhibitory interaction: the PACT-binding motif (PBM) in PKR's kinase domain normally interacts with PKR's dsRNA-binding domain to maintain an inactive conformation; binding of PACT or dsRNA, or a decoy PBM peptide, disrupts this interaction to activate PKR. Identified by NMR analysis combined with biochemical and genetic validation. NMR, biochemical interaction assays, point mutagenesis producing constitutively active PKR, decoy peptide assay Proceedings of the National Academy of Sciences of the United States of America High 16785445
2006 PACT is a component of the ~500 kDa RISC complex containing Dicer, hAgo2, and TRBP. PACT interacts with Dicer via its third dsRNA-binding domain (dsRBD) and Dicer's N-terminal helicase motif. Depletion of PACT strongly reduces mature miRNA accumulation in vivo and moderately reduces siRNA-induced RNAi efficiency, indicating a role in RISC assembly distinct from pre-miRNA cleavage. Co-immunoprecipitation, size-exclusion chromatography, siRNA depletion, Northern blot for mature miRNA The EMBO journal High 16424907
2006 RAX/PACT interaction with PKR is required for PKR activation and consequent eIF2α phosphorylation in response to a broad range of stresses (serum deprivation, IFNγ/TNFα, chemotherapy, viral infection); RAX knockdown (80%) prevents PKR activation and IκB degradation, IRF-1 expression, and STAT1 phosphorylation; non-phosphorylatable RAX(S18A) acts as dominant negative blocking PKR-dependent apoptosis. siRNA knockdown, dominant-negative mutant expression, kinase activity assay, Western blot for signaling intermediates Blood High 16861340
2006 RAX/PACT interaction with PKR modulates ethanol-induced inhibition of protein synthesis and neuronal cell death: ethanol promotes PKR-RAX association in cells expressing wild-type RAX but not RAX(S18A); overexpression of wild-type RAX enhances ethanol-induced PKR/eIF2α phosphorylation and cell death, while RAX(S18A) blocks it. Co-immunoprecipitation, kinase assay, dominant-negative expression, PKR-null cells, translation assay The Journal of biological chemistry High 16574643
2008 A homozygous missense mutation (P222L) in PRKRA segregates with an autosomal recessive dystonia-parkinsonism syndrome (DYT16) in two unrelated families, identifying PRKRA as the causative gene for this movement disorder at chromosome 2q31.2. Autozygosity mapping (high-density SNP genotyping), candidate gene sequencing, segregation analysis The Lancet. Neurology High 18243799
2008 TRBP controls PACT-induced PKR activation: TRBP and PACT interact through their dsRBDs and Medipal domains; TRBP inhibits PACT-induced PKR phosphorylation in cells with high TRBP levels; stress stimuli (arsenite, peroxide, serum starvation) dissociate the TRBP-PACT interaction and restore PACT-induced PKR activation. Demonstrated in TRBP-null fibroblasts and by siRNA knockdown. Co-immunoprecipitation, yeast two-hybrid, TRBP-null cells, siRNA knockdown, PKR phosphorylation assay Molecular and cellular biology High 18936160
2008 PACT is required for postnatal anterior pituitary lobe proliferation: Pact−/− mice develop anterior pituitary hypoplasia postnatally with reduced numbers of corticotrophs, gonadotrophs, somatotrophs, and especially lactotrophs, due to decreased cell proliferation (not increased apoptosis). siRNA knockdown of PACT in pituitary cell lines recapitulates the proliferation defect in vitro. Knockout mouse phenotyping, cell counting/histology, BrdU proliferation assay, siRNA knockdown in cell lines Proceedings of the National Academy of Sciences of the United States of America High 19541653
2008 Rax/RAX (PRKRA) knockout in mice causes embryonic lethality at a preimplantation stage; in Drosophila, loss of dRax (loqs/R3D1) causes abnormal CNS commissural axon structure, lethality in 70% of homozygotes, and reduced locomotion, demonstrating RAX is essential for embryonic development in two species. Mouse gene knockout (no viable homozygous null at E3.5–14), Drosophila transposon insertion mutant analysis, behavioral assay Mechanisms of development Medium 18634873
2009 Stress-induced phosphorylation of PACT at Ser246 and Ser287 (phosphomimetic aspartate substitutions) increases PACT's affinity for PKR in vitro, leading to more efficient PKR activation and eIF2α phosphorylation; inactive PACT mutants bind PKR with lower affinity. In vitro kinase assay with phosphomimetic mutants, binding affinity measurement, eIF2α phosphorylation Biochemistry High 19580324
2011 PACT physically binds the C-terminal repression domain of RIG-I and potently stimulates RIG-I-induced type I interferon production; PACT potentiates activation by intermediate-length poly(I:C) and stimulates RIG-I's ATPase activity through direct interaction, independently of dsRNA, PKR, or Dicer; PACT depletion substantially attenuates viral induction of interferons. Co-immunoprecipitation, ATPase assay, siRNA depletion, interferon reporter assay Cell host & microbe High 21501829
2011 miR-122 directly targets the 3'-UTR of PRKRA and suppresses PACT expression in human hepatic stellate cells; reduced PACT expression (by miR-122 or siRNA) suppresses NF-κB nuclear translocation and production of proinflammatory cytokines (IL-6, MCP-1, IL-1β). Luciferase 3'-UTR reporter assay, siRNA knockdown, NF-κB immunofluorescence, cytokine ELISA Nucleic acids research Medium 21937511
2011 PACT becomes a PKR inhibitor during HIV-1 replication: in HIV-1-infected lymphocytic cells, PACT participates in a multiprotein complex with ADAR1 around PKR and inhibits PKR and eIF2α phosphorylation, increasing HIV-1 protein expression and virion production; this contrasts with PACT's normal activating role and depends partly on PACT interaction with ADAR1 (in the absence of RNA). Co-immunoprecipitation, PKR phosphorylation assay, HIV-1 virion production measurement, shRNA knockdown, cell-line-specific comparisons Retrovirology Medium 24020926
2011 Stress-induced phosphorylation of PACT at Ser287 significantly increases PACT's ability to activate PKR by weakening its interaction with TRBP; a non-phosphorylatable S287A mutant causes enhanced TRBP-PACT interaction and loss of PKR activation; TRBP overexpression cannot block apoptosis induced by a phosphomimetic constitutively active PACT mutant. Site-directed mutagenesis, co-immunoprecipitation, PKR activation assay, apoptosis assay Biochemistry High 21526770
2012 Enhanced PACT-PACT homodimerization upon phosphorylation at Ser246 and Ser287 is essential for efficient PKR activation in response to stress; a PACT point mutant deficient in PACT-PACT interaction fails to activate PKR efficiently even when phosphorylated. Co-immunoprecipitation, point mutagenesis disrupting homodimerization, PKR kinase assay Journal of cellular biochemistry Medium 22473766
2012 The RAX/PACT–PKR stress response pathway promotes p53 sumoylation: RAX/PACT interacts with SUMO E2 ligase Ubc9 to stimulate p53-Ubc9 association and reversible p53 sumoylation on Lys386; this leads to p53 stability, enhanced p53 target gene expression, and G1 arrest only when both PKR and sumoylation are functional. Co-immunoprecipitation, sumoylation assay, cell cycle analysis (FACS), p53 target gene expression, dominant-negative PKR, SENP1 desumoylase overexpression Cell cycle Medium 22214662
2013 PACT and TRBP have distinct effects on Dicer-mediated dsRNA processing: PACT-Dicer complex inhibits pre-siRNA processing compared with Dicer or Dicer-TRBP; PACT and TRBP show non-redundant effects on miRNA isomiR production, altering target-binding specificities; chimeric protein experiments show the two N-terminal RNA-binding domains of each protein confer the differences. Reconstituted in vitro cleavage assay with purified proteins, chimeric protein domain swap, isomiR sequencing Nucleic acids research High 23661684
2013 EBOV VP35 inhibits PACT-induced RIG-I ATPase activity in a dose-dependent manner; VP35 disrupts the PACT-RIG-I interaction; PACT-VP35 interaction also impairs VP35 association with the viral polymerase, diminishing viral RNA synthesis; PACT-deficient cells are defective in IFN induction and insensitive to VP35 function, demonstrating mutual antagonism between VP35 and PACT. Co-immunoprecipitation, ATPase assay, siRNA/PACT-KO cells, viral RNA synthesis assay, IFN reporter Cell host & microbe High 23870315
2013 PACT is required for HSV-1-induced type I interferon production: Us11 associates tightly with PACT to prevent it from binding and activating RIG-I; Us11-deficient HSV-1 is indistinguishable from Us11-proficient virus when PACT is compromised; HSV-1-induced IFN production is abrogated in PACT knockout MEFs. Co-immunoprecipitation, PACT-knockout MEFs, interferon production assay, Us11-deficient virus comparison Journal of virology High 24067967
2013 TRBP binds siRNA as a monomer with high affinity (higher than its homodimerization affinity), while PACT preferentially homodimerizes over siRNA binding; this distinction means siRNA is more readily incorporated into RISC via TRBP than PACT in vivo. Electrophoresis mobility shift assay (EMSA), gel filtration chromatography, in vitro binding analysis PloS one Medium 23658827
2014 DYT16 dystonia is confirmed in a European (Polish) family carrying the same homozygous P222L PRKRA mutation at chromosome 2q31.2 as the original Brazilian cases, independently replicating the locus; three novel heterozygous PRKRA changes were found in isolated focal/segmental dystonia patients. Whole-exome sequencing, homozygosity mapping, Sanger sequencing, high-resolution melting analysis Movement disorders High 25142429
2015 PACT is an essential coactivator of MDA5: virus-induced and poly(I:C)-induced activation of MDA5 is severely impaired in PACT-knockout cells; PACT promotes dsRNA-induced oligomerization of MDA5 (filament assembly), facilitates MDA5 recruitment to dsRNA ligand, and co-localizes with MDA5 in the cytoplasm; PACT had no effect on MDA5 mutants deficient for oligomerization. PACT-knockout cells, interferon reporter assay, MDA5 oligomerization assay, co-localization (immunofluorescence), co-immunoprecipitation Journal of immunology High 28760879
2015 DDX3 facilitates translation of PACT mRNA (which contains a structured 5' UTR), thereby supporting antiviral innate immunity; DDX3 knockdown decreases PACT protein levels and reduces viral RNA detection sensitivity; PACT partially rescues IFN-β and RANTES induction defects in DDX3-knockdown cells; HCV core protein sequesters DDX3 in stress granules, inhibiting PACT mRNA translation. siRNA knockdown, reporter assay for PACT 5' UTR translation, IFN-β/RANTES measurement, co-localization The FEBS journal Medium 26454002
2015 PACT-mediated PKR activation is required for postnatal anterior pituitary proliferation: RAX/PKR double-knockout mice show rescue of the rax−/− developmental defects (reduced body size, pituitary hypoplasia, fertility defects); kinase-inactive PKR(K271R) also rescues rax−/− phenotype; heterozygous unphosphorylatable eIF2α(S51A) provides partial rescue; RAX knockdown in pituitary cells increases PKR activity and p21 induction. This unexpectedly identifies RAX as a negative regulator of PKR in pituitary tissue. Double-knockout mouse genetics, kinase-dead PKR knock-in, eIF2α(S51A) heterozygous rescue, siRNA in pituitary cell lines, p21 expression assay The FEBS journal High 26414443
2015 PRKRA/PACT promotes chemoresistance of mucinous ovarian cancer via its Dicer interaction: PRKRA siRNA combined with oxaliplatin shows antitumor effect in orthotopic mouse models; PACT-Dicer interaction regulates miR-515-3p expression, which in turn sensitizes cells to oxaliplatin by targeting AXL. siRNA kinome screen, orthotopic mouse model, miRNA expression analysis, luciferase reporter, AXL expression analysis Molecular cancer therapeutics Medium 30305341
2017 MHV and SARS-CoV nucleocapsid proteins antagonize IFN-β production by directly interacting with PACT, sequestering PACT from RIG-I and MDA5 and thereby inhibiting IFN-β production; this mechanism is not shared by PEDV or PRRSV N proteins. Co-immunoprecipitation, IFN-β reporter assay, RIG-I/MDA5-PACT interaction disruption assay Oncotarget Medium 28591694
2017 LGP2 directly interacts with PACT via LGP2's regulatory C-terminal domain; this LGP2-PACT interaction is necessary for LGP2-mediated inhibition of RIG-I-dependent responses and for amplification of MDA5-dependent responses; a single point mutation in LGP2 that disrupts LGP2-PACT interaction abolishes both regulatory effects. Co-immunoprecipitation, point mutagenesis, IFN reporter assay, siRNA knockdown, protein-protein interaction mapping Science signaling High 31575732
2017 Luteolin inhibits the PKR-PACT interaction at their dsRNA-binding domains (identified by HTRF screen validated by NanoLuc complementation assay); luteolin inhibits PKR phosphorylation, the integrated stress response, and induction of pro-inflammatory cytokines in macrophages under oxidative stress and TLR stimulation, in a PKR-dependent manner. HTRF high-throughput screening, NanoLuc protein complementation, PKR phosphorylation assay, cytokine measurement in macrophages Scientific reports Medium 29170442
2018 Arenaviral nucleoproteins suppress PACT-induced RIG-I activation to inhibit type I IFN production; NP RNase activity degrades PAMP RNA rather than directly disrupting PACT-RIG-I interaction (different mechanism from other viral proteins); PACT-KO MEFs show increased arenavirus replication, confirming PACT's role in restricting arenavirus. PACT-KO MEFs, RIG-I-KO MEFs, recombinant virus growth kinetics, IFN measurement, NP RNase mutant analysis Journal of virology Medium 29669840
2019 PDCoV nucleocapsid protein antagonizes IFN-β by interacting with RIG-I and MDA5, interfering with binding of both dsRNA and PACT to RIG-I, thereby preventing RIG-I activation. Co-immunoprecipitation, IFN-β reporter assay, dsRNA/PACT competition binding assay Virus genes Medium 31129785
2019 A frameshift (FS) DYT16 PACT mutant protein loses dsRNA binding and PKR interaction but retains PACT-PACT and TRBP interactions; when expressed, it aggregates and triggers caspase-mediated apoptosis both PKR/PACT-dependently (by displacing PACT from TRBP, enabling endogenous PACT to activate PKR) and independently; interaction of FS mutant with TRBP dissociates PACT from the TRBP-PACT complex. Co-immunoprecipitation, dsRNA binding assay, caspase activation assay, fluorescent protein fusion aggregation imaging, PKR-null cells Journal of cellular biochemistry Medium 31246344
2020 DYT16 PRKRA mutations (P222L and four others) cause stronger PACT-PACT interactions and enhanced PKR activation in vitro and in patient-derived lymphoblasts; DYT16 lymphoblasts show dysregulated ISR and increased apoptosis in response to ER stress; luteolin (PACT-PKR interaction inhibitor) rescues the enhanced ER stress sensitivity. Co-immunoprecipitation, kinase assay, patient lymphoblast ISR analysis (eIF2α phosphorylation), apoptosis assay, luteolin pharmacological rescue Neurobiology of disease High 33049316
2020 PACT-mediated PKR activation acts as a hyperosmotic stress intensity sensor: high osmotic stress activates PACT-PKR, which inhibits the interaction between NF-κB c-Rel and TonEBP (needed for osmoprotective gene expression), driving formation of TonEBP/NF-κB p65 complexes and proinflammatory gene expression instead. PACT-PKR knockdown/activation, co-immunoprecipitation of Rel family dimers, osmotic stress assays in MEFs, TonEBP target gene expression eLife Medium 32175843
2025 PACT functions as a key inhibitor of PKR during viral infection (identified by genome-wide CRISPR-Cas9 screen), suppressing PKR hyperactivation; PACT cooperates with ADAR1 to suppress PKR activation by endogenous self-dsRNAs in uninfected cells; simultaneous deletion of PACT and ADAR1 causes synthetic lethality that is fully rescued in PKR-deficient cells. CRISPR-Cas9 genome-wide knockout screen (CRISPR-Translate), double-knockout cell lines, PKR-KO rescue, translation assay Nature communications High 40185749
2008 PACT is essential for PKR-mediated apoptosis induced by tunicamycin (ER stress): PACT is phosphorylated in response to tunicamycin and directly activates PKR; PACT-null and PKR-null cells are markedly resistant to tunicamycin with defective eIF2α phosphorylation and CHOP induction; reconstitution of PACT and PKR expression restores sensitivity. PACT-null and PKR-null cells, reconstitution, eIF2α phosphorylation, CHOP expression, apoptosis assay Journal of molecular biology High 19007793
2017 ADAR1 and PACT contribute to efficient translation of HIV-1 TAR-containing transcripts: interactions between PACT, ADAR1, and viral Tat protein diminish PKR activation in response to HIV-1 infection; demonstrated by reporter systems and in vitro kinase assays. Reporter assay, in vitro kinase assay, co-immunoprecipitation The Biochemical journal Medium 28167698

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2861 17081983
2005 A human protein-protein interaction network: a resource for annotating the proteome. Cell 1704 16169070
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2016 ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 1233 26777405
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2014 A proteome-scale map of the human interactome network. Cell 977 25416956
2012 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Molecular cell 973 22681889
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2007 Large-scale mapping of human protein-protein interactions by mass spectrometry. Molecular systems biology 733 17353931
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