Affinage

HJURP

Holliday junction recognition protein · UniProt Q8NCD3

Length
748 aa
Mass
83.5 kDa
Annotated
2026-06-10
48 papers in source corpus 28 papers cited in narrative 30 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HJURP is the CENP-A-specific histone chaperone that defines and propagates centromere identity by depositing newly synthesized CENP-A nucleosomes during early G1 (PMID:19410544, PMID:19410545). It recognizes CENP-A through a conserved N-terminal CENP-A-binding domain that engages the CENP-A/H4 heterodimer at a CENP-A-specific surface centered on the CATD, with the TLTY box essential for complex formation and the C-terminal β-sheet domain capping the histone DNA-binding surface to prevent premature chromatin association (PMID:20080577, PMID:21478274, PMID:22406139); HJURP dimerizes through its C terminus to assemble octameric CENP-A nucleosomes, an activity separable from centromere recruitment and CENP-A binding (PMID:23771058). HJURP is sufficient to build a functional de novo centromere when ectopically targeted, establishing it as the central chromatin-assembly factor of centromere inheritance (PMID:21768289). Its centromeric arrival is gated to G1 by two parallel recruitment routes—the Mis18α/Mis18β/M18BP1 complex, engaged through interchangeable HJURP repeats and an M18BP1 contact, and direct binding to the CENP-C C-terminal domain—both of which are required and which CDK phosphorylation suppresses outside G1 by weakening Mis18β binding and blocking CENP-C interaction in metaphase (PMID:24519934, PMID:26063729, PMID:31492860, PMID:37141119). Beyond deposition, HJURP recruits condensin II to drive the chromatin decondensation that accompanies CENP-A loading and, during S phase, cooperates with the MCM2-7 helicase to retain pre-existing CENP-A nucleosomes through replication (PMID:27807043, PMID:30293838). Outside centromere biology, HJURP is recruited to DNA double-strand breaks in a PARylation-dependent manner where it promotes H3K9me3/HP1 turnover to facilitate repair (PMID:38279062), forms disulfide intermediates with PRDX1 to enhance its peroxidase activity and suppress ferroptosis (PMID:39405980), and is overexpressed in cancers where it destabilizes p21 (PMID:30111352, PMID:34099634).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 2009 High

    Established HJURP as the dedicated CENP-A chaperone, answering how new CENP-A is specifically deposited at centromeres during the cell cycle.

    Evidence Co-IP/MS of prenucleosomal complexes, RNAi with centromeric CENP-A quantification and cell-cycle analysis in human cells

    PMID:19410544 PMID:19410545

    Open questions at the time
    • Did not resolve the structural basis of CENP-A discrimination
    • Mechanism of centromere targeting not defined
  2. 2010 High

    Reconstituted the minimal deposition reaction, showing HJURP's N-terminal domain binds CENP-A/H4 selectively and deposits it onto DNA, proving direct chaperone activity.

    Evidence Bacterial expression, stoichiometric pull-downs, in vitro DNA deposition, TLTY-box mutagenesis

    PMID:20080577

    Open questions at the time
    • Octamer assembly versus tetramer deposition not addressed
    • No structure of the binding interface
  3. 2010 High

    Linked a chromatin mark to chaperone recruitment, showing centromeric H3K4me2 and transcription are needed for HJURP loading.

    Evidence LSD1 tethering to a human artificial chromosome, ChIP and centromere function assays

    PMID:21157429

    Open questions at the time
    • Direct molecular link between H3K4me2 and HJURP not defined
    • Whether transcription or the mark per se is the signal unresolved
  4. 2011 High

    Demonstrated HJURP is sufficient to seed a functional centromere and depends on the Mis18 complex for endogenous recruitment, defining it as the central epigenetic assembly factor.

    Evidence LacI-LacO ectopic targeting, in vitro chromatin assembly, kinetochore readouts, Mis18 RNAi

    PMID:21768289

    Open questions at the time
    • Direct HJURP–Mis18 contacts not mapped
    • How recruitment is timed to G1 unresolved
  5. 2011 High

    Solved the structural basis of CENP-A recognition, showing HJURP caps the histone DNA-binding surface and exploits a CENP-A-specific site to exclude H3.

    Evidence X-ray crystallography of HJURP–CENP-A–H4 with mutagenesis

    PMID:21478274

    Open questions at the time
    • Did not capture the dimeric assembly-competent state
    • How capping is released for DNA loading not shown
  6. 2011 High

    Confirmed deposition activity is conserved and identified condensin II as a co-requirement, using a cell-free system that recapitulates loading specificity.

    Evidence Xenopus egg extract deposition, immunodepletion, human HJURP complementation, condensin-selective depletion

    PMID:21321101

    Open questions at the time
    • Mechanism by which condensin II aids loading not defined
    • HJURP–condensin physical link not shown here
  7. 2012 High

    Dissected CATD recognition versus stabilization, distinguishing surface residues read by HJURP from buried residues that confer post-assembly stability.

    Evidence Structure-guided mutagenesis of CENP-A/HJURP surfaces, in vitro binding, in-cell incorporation

    PMID:22406139

    Open questions at the time
    • How stability is transmitted to chromatin not fully resolved
    • Role of CENP-A/CENP-A interface in HJURP handoff unclear
  8. 2013 High

    Identified HJURP homodimerization via the C-terminal domain as required for nucleosome assembly but not for recruitment or CENP-A binding, separating assembly from targeting.

    Evidence Crystallography, gel filtration, cross-linking, separation-of-function mutants in cells

    PMID:23771058

    Open questions at the time
    • How dimerization couples two CENP-A/H4 dimers into an octamer not shown
    • Trigger for dimer-dependent assembly unknown
  9. 2014 High

    Defined cell-cycle gating, showing CDK phosphorylation prevents premature centromere recruitment while a DNA-binding domain drives deposition once HJURP arrives.

    Evidence Phosphosite mapping, phospho-mutants, cell-cycle imaging, in vitro DNA binding

    PMID:24519934 PMID:25001279

    Open questions at the time
    • Full set of relevant phosphosites incomplete
    • How dephosphorylation is timed to G1 not defined
  10. 2015 High

    Mapped HJURP–M18BP1 association and revealed a CENP-A-independent centromere expansion activity, broadening HJURP's recruitment interactions and functions.

    Evidence Co-IP, DT40 knockout/gene replacement with domain mutants, ectopic targeting

    PMID:26063729

    Open questions at the time
    • Molecular basis of expansion activity unknown
    • Relationship between expansion and deposition unresolved
  11. 2016 High

    Established a physical and functional HJURP–condensin II link, showing HJURP recruits CAPH2 to drive decondensation required for CENP-A deposition.

    Evidence Condensin I/II-selective Co-IP, CAPH2 imaging, LacO decondensation assay, RNAi with CENP-A readout

    PMID:27807043

    Open questions at the time
    • How decondensation promotes loading mechanistically unclear
    • Timing relative to Mis18-dependent recruitment not resolved
  12. 2018 High

    Extended HJURP's role to S phase, showing it cooperates with MCM2-7/MCM2 to retain parental CENP-A nucleosomes through replication.

    Evidence S-phase BioID, reciprocal Co-IP with MCM2-7, CENP-A retention assays after replication

    PMID:30293838

    Open questions at the time
    • How parental CENP-A is handed back to daughter strands not shown
    • Coordination with G1 deposition machinery unclear
  13. 2019 High

    Resolved the stoichiometry of HJURP engagement with the Mis18 complex, showing two interchangeable HJURP repeats bind the assembled complex without dissociating it.

    Evidence Reconstitution of Mis18 complex with HJURP repeats, photo-cross-linking, mutagenesis, in-cell recruitment

    PMID:31492860

    Open questions at the time
    • How two CENP-A/H4 dimers are assembled into a tetramer in vivo not directly shown
    • Coordination with CENP-C pathway unaddressed
  14. 2023 High

    Revealed a second layer of cell-cycle gating, showing phosphorylation blocks HJURP–CENP-C interaction and M18BP1.S competes for CENP-C to prevent ectopic metaphase assembly.

    Evidence Xenopus egg extract assembly, phospho-mutants, HJURP–CENP-C Co-IP, M18BP1.S competition

    PMID:37141119

    Open questions at the time
    • Kinase responsible for the CENP-C-blocking phosphorylation not pinned down
    • Interplay between CENP-C and Mis18 routes not resolved here
  15. 2025 Medium

    Defined CENP-C and Mis18 as dual parallel recruitment pathways, showing direct HJURP–CENP-C CTD binding is required and that abolishing both pathways fully blocks CENP-A loading.

    Evidence In vitro binding, DT40 complementation with CENP-C-binding mutants, Mis18 knockout combination, chromatin Co-IP (preprint)

    Open questions at the time
    • Preprint, not yet peer-reviewed
    • How the two pathways are temporally coordinated not resolved
  16. 2024 Medium

    Extended HJURP beyond centromeres to DNA repair, showing PARylation-dependent recruitment to double-strand breaks where it turns over H3K9me3/HP1.

    Evidence Laser micro-irradiation, PARP-inhibitor dependency, ChIP for H3K9me3/HP1, clonogenic survival in glioma cells

    PMID:38279062

    Open questions at the time
    • Single lab; whether chaperone activity is required at DSBs unclear
    • Direct partner at DSBs not identified
  17. 2024 High

    Identified a redox role, showing HJURP forms disulfide intermediates with PRDX1 to enhance its peroxidase activity and suppress ferroptosis.

    Evidence Co-IP, disulfide crosslinking, Cys327/Cys457 mutagenesis, peroxidase and ferroptosis assays in prostate cancer

    PMID:39405980

    Open questions at the time
    • Relationship to nuclear chaperone function unknown
    • Whether this is cancer-specific not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How HJURP's centromeric, replication-fork, DNA-repair, and redox/oncogenic activities are partitioned within a cell, and how its many recruitment routes are integrated into a single timed deposition program, remains unresolved.
  • No unified model coupling centromere and non-centromere functions
  • Kinase/phosphatase circuitry controlling timing incompletely mapped
  • Cancer roles (p21, YAP1, ferroptosis) mechanistically separable from chaperone activity not clarified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0042393 histone binding 5 GO:0140096 catalytic activity, acting on a protein 3 GO:0003677 DNA binding 2
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 2
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-4839726 Chromatin organization 3 R-HSA-73894 DNA Repair 1
Partners
CENPACENPCH4M18BP1MCM2MIS18BPRDX1YWHA (14-3-3)
Complex memberships
HJURP–CENP-A–H4 prenucleosomal complexMCM2-7 helicase complexMis18 complex (Mis18α/Mis18β/M18BP1) co-complex

Evidence

Reading pass · 30 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 HJURP forms a prenucleosomal complex with CENP-A, histone H4, and nucleophosmin 1, and is required for recruitment of new CENP-A into nucleosomes at replicated centromeres during G1 phase. Recognition by HJURP is mediated through the centromere targeting domain (CATD) of CENP-A. Co-immunoprecipitation, mass spectrometry, RNAi knockdown with centromeric CENP-A quantification, cell-cycle analysis Cell High 19410544
2009 HJURP is specifically found in CENP-A-containing non-nucleosomal complexes but not in H3.1- or H3.3-containing complexes, indicating specificity for CENP-A. HJURP centromeric localization is cell-cycle regulated, transiently appearing at centromeres coinciding with the window of new CENP-A deposition. HJURP downregulation causes major reduction in centromeric CENP-A and impairs deposition of newly synthesized CENP-A, causing mitotic defects. Biochemical purification of non-nucleosomal CENP-A complexes, Co-IP, RNAi knockdown, immunofluorescence, cell-cycle analysis Cell High 19410545
2010 Bacterially expressed HJURP binds the CENP-A/H4 tetramer but not the H3/H4 tetramer at a stoichiometric ratio. Binding occurs through a conserved N-terminal domain of HJURP (the CENP-A binding domain, CBD), and the TLTY box within this domain is essential for HJURP–CENP-A/H4 complex formation. HJURP facilitates efficient deposition of CENP-A/H4 tetramers onto naked DNA in vitro. Bacterial expression, pull-down binding assays, in vitro chromatin deposition assay, mutational analysis of the TLTY box Proceedings of the National Academy of Sciences of the United States of America High 20080577
2010 H3K4me2 at the centromere is required for efficient HJURP recruitment and subsequent CENP-A incorporation. Specific depletion of H3K4me2 using tethered LSD1 demethylase from a synthetic human artificial chromosome caused loss of centromeric transcription and failure to recruit HJURP, leading to gradual CENP-A loss and kinetochore inactivation. Epigenetic tethering (LSD1-LacI fusion to HAC LacO array), ChIP, immunofluorescence, centromere function assays The EMBO journal High 21157429
2011 HJURP is a chromatin assembly factor sufficient to drive stable recruitment of CENP-A to a noncentromeric LacO array when fused to LacI, and an amino-terminal fragment of HJURP assembles CENP-A nucleosomes in vitro. Ectopically targeted CENP-A chromatin is sufficient to direct assembly of a functional centromere including kinetochore proteins and stable kinetochore-microtubule attachments. HJURP recruitment to endogenous centromeres requires the Mis18 complex. LacI-LacO tethering assay, in vitro chromatin assembly with recombinant N-terminal HJURP fragment, immunofluorescence, kinetochore assembly readouts (NDC80 recruitment, microtubule attachment), RNAi of Mis18 complex components The Journal of cell biology High 21768289
2011 Crystal structure of an HJURP–CENP-A–histone H4 complex shows that HJURP binds a CENP-A–H4 heterodimer. The C-terminal β-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing spontaneous DNA association. A novel site in CENP-A distinguishes it from histone H3 in its ability to bind HJURP. X-ray crystallography of HJURP–CENP-A–H4 complex, structural analysis and mutagenesis Genes & development High 21478274
2011 Xenopus HJURP (xHJURP), a member of the HJURP/Scm3 family, is required for CENP-A deposition in a Xenopus egg extract system that recapitulates spatial and temporal specificity of CENP-A loading. Human HJURP can substitute for xHJURP despite little sequence homology. Condensin II (but not condensin I) is also required for CENP-A assembly and contributes to retention of centromeric CENP-A nucleosomes. Xenopus egg extract in vitro CENP-A deposition assay, immunodepletion, complementation with human HJURP, condensin I/II-selective depletion The Journal of cell biology High 21321101
2012 Surface-exposed residues in the CENP-A targeting domain (CATD) are the primary sequence determinants for HJURP recognition, while buried CATD residues generating rigidity with H4 are also required for efficient centromeric incorporation. HJURP contact points adjacent to the CATD transmit stability throughout the histone fold domains of CENP-A and H4. An intact CENP-A/CENP-A interface is required for stable chromatin incorporation immediately upon HJURP-mediated assembly. Structure-guided mutagenesis of CENP-A and HJURP contact surfaces, in vitro binding assays, centromere incorporation assays in cells Developmental cell High 22406139
2013 HJURP forms a homodimer through its C-terminal domain (including the second HJURP_C domain). HJURP exists as a dimer in the soluble pre-assembly complex and at chromatin during new CENP-A deposition. Dimerization is essential for deposition of new CENP-A nucleosomes but is not required for HJURP recruitment to centromeres or CENP-A binding. Crystallographic and biochemical analysis of HJURP dimerization domain, gel filtration, cross-linking, separation-of-function mutants in cells, centromeric CENP-A quantification The EMBO journal High 23771058
2014 Cell-cycle-dependent recruitment of HJURP to centromeres depends on its phosphorylation by cyclin-dependent kinases. A nonphosphorylatable HJURP mutant localizes prematurely to centromeres in S and G2 phase, causing premature CENP-A loading and cell-cycle delays. Once at centromeres, HJURP promotes CENP-A deposition through a DNA-binding domain. Phosphosite mapping, nonphosphorylatable/phosphomimetic HJURP mutants, immunofluorescence, cell-cycle analysis, in vitro DNA-binding assay Cell reports High 25001279
2014 Human HJURP directly binds Mis18β through a minimal region mapping to residues 437–460. Depletion of Mis18β by RNAi dramatically impairs HJURP recruitment to centromeres. CDK1 phosphorylation of HJURP weakens its interaction with Mis18β, linking cell-cycle regulation to CENP-A deposition timing. Co-IP, GST pulldown, domain mapping, RNAi depletion of Mis18β, CDK1 phosphorylation assay, immunofluorescence The Journal of biological chemistry High 24519934
2015 The middle region of HJURP associates with the Mis18 complex protein M18BP1/KNL2, and the HJURP–M18BP1 association is required for HJURP function. HJURP also exhibits a centromere expansion activity separable from its CENP-A-binding activity, demonstrated by ectopic HJURP localization inducing expansion of artificial and natural centromeres. Co-IP, DT40 knockout cell lines, gene replacement with domain mutants, ectopic HJURP localization assay, immunofluorescence of centromere size Molecular biology of the cell High 26063729
2016 HJURP selectively associates with the condensin II complex (not condensin I) during G1, recruits condensin II subunit CAPH2 to centromeres at the time of CENP-A deposition, and induces decondensation of a noncentromeric LacO array. Condensin II function at the centromere is required for new CENP-A deposition in human cells. Co-IP distinguishing condensin I vs. II, immunofluorescence of CAPH2 centromere localization, LacO/LacI decondensation assay, RNAi of CAPH2, CENP-A incorporation quantification Molecular biology of the cell High 27807043
2018 During S phase, HJURP transiently associates with centromeres and binds pre-existing CENP-A, and is required for centromeric nucleosome inheritance during DNA replication. HJURP co-purifies with the MCM2-7 helicase complex and, together with the MCM2 subunit, binds CENP-A simultaneously, suggesting a mechanism for parental CENP-A retention at the replication fork. BioID proximity labeling during S phase, co-immunoprecipitation of HJURP with MCM2-7, CENP-A retention assays after replication, HJURP depletion with S-phase-specific readouts Developmental cell High 30293838
2018 HJURP antagonizes ectopic CENP-A deposition driven by H3.3 chaperones HIRA and DAXX; the correct balance between HJURP and CENP-A levels is essential to preclude ectopic assembly by H3.3 chaperones. RNAi knockdown of HJURP, HIRA, and DAXX in human cancer cells; ChIP and immunofluorescence to quantify ectopic CENP-A; epistasis analysis PloS one Medium 30365520
2019 Two repeats in human HJURP proposed to be functionally distinct are in fact interchangeable and bind concomitantly to the 4:2:2 Mis18α:Mis18β:M18BP1 complex without dissociating it. HJURP binds CENP-A:H4 dimers, requiring two Mis18αβ:M18BP1:HJURP complexes (or consecutive rounds by the same complex) to assemble CENP-A:H4 tetramers. Mis18α N-terminal tails blockade two identical HJURP-repeat binding sites near Mis18αβ C-terminal helices, identified by photo-cross-linking and mutated to separate Mis18 from HJURP centromere recruitment. Biochemical reconstitution of Mis18 complex with HJURP repeats, photo-cross-linking, mutational analysis, in-cell centromere recruitment assays Nature communications High 31492860
2019 CENP-A nucleosomes form characteristic rosette-like clusters (~250–300 nm) during G1, with HJURP located at the center of each rosette serving as a nucleation point for CENP-A assembly, as revealed by 2D/3D super-resolution microscopy. 2D and 3D super-resolution microscopy (dSTORM/PALM), segmentation analysis, co-localization of HJURP and CENP-A Nature communications Medium 31570711
2020 The yeast HJURP ortholog Scm3 acts as a cochaperone with the ATAD2 homolog Yta7 for Cse4(CENP-A) deposition; Yta7 interacts in vivo with Scm3 and increased Cse4 deposition caused by Yta7 overexpression requires Scm3 activity. Co-immunoprecipitation of Scm3 with Yta7, genetic epistasis (Yta7 OE requires Scm3), ChIP of centromeric Cse4, chromosome segregation assays in yeast Proceedings of the National Academy of Sciences of the United States of America Medium 32079723
2020 The critical residues mediating CENP-A–HJURP interaction differ between chicken and human; the A59Q mutation in chicken CENP-A α1-helix causes CENP-A misincorporation and cell death, whereas the corresponding human mutation does not. W53 of chicken HJURP (a contact site for A59) is also essential. Introduction of two arginine residues to the chicken HJURP αA-helix suppresses CENP-A misincorporation, revealing species-specific affinity tuning of the CENP-A–HJURP interface. Point mutagenesis of chicken and human CENP-A and HJURP, DT40 cell complementation assays, cell viability, immunofluorescence of CENP-A incorporation Cell reports High 33207191
2007 HJURP (then called FAKTS) localizes to the nucleus and interacts with 14-3-3 proteins in mammalian cells. This interaction is enhanced by activated Akt/PKB and is dependent on phosphorylation of Ser479 by AKT/PKB. Yeast two-hybrid screen, confocal microscopy, co-immunoprecipitation in mammalian cells, Akt overexpression, Ser479 mutational analysis Proteins Medium 17256767
2013 HJURP knockdown in human dermal fibroblasts and endothelial cells leads to premature cellular senescence via a p53-dependent pathway; p53 knockdown, but not p16 knockdown, abolishes the senescence phenotype caused by HJURP reduction. RNAi knockdown of HJURP, ectopic HJURP overexpression in senescent cells, p53 and p16 siRNA epistasis, senescence assays (SA-β-gal, proliferation) The journals of gerontology. Series A, Biological sciences and medical sciences Medium 23292286
2023 HJURP phosphorylation prevents its interaction with CENP-C in metaphase, blocking delivery of soluble CENP-A to centromeres. Non-phosphorylatable HJURP mutants constitutively bind CENP-C in metaphase but are insufficient alone for CENP-A assembly. M18BP1.S also binds CENP-C to competitively inhibit HJURP access to centromeres in metaphase. Removal of both inhibitory activities causes ectopic CENP-A assembly in metaphase. Cell-free Xenopus egg extract centromere assembly assay, phospho-mutant HJURP, co-immunoprecipitation of HJURP with CENP-C, M18BP1.S competition experiments The Journal of cell biology High 37141119
2018 HJURP destabilizes p21 (CDKN1A) in hepatocellular carcinoma cells via MAPK/ERK1/2 and AKT/GSK3β pathways, promoting nucleus-to-cytoplasm translocation and ubiquitin-mediated degradation of p21. HJURP silencing effects on cell growth are reversed by p21 knockdown. Co-immunoprecipitation, Western blot for p21 stability, immunofluorescence of p21 localization, ERK1/2 inhibitor (U0126) and AKT agonist (SC-79) treatment, ubiquitination assay, genetic epistasis (HJURP KD + p21 KD) Journal of experimental & clinical cancer research : CR Medium 30111352
2021 HJURP increases ubiquitination of CDKN1A (p21) via the GSK3β/JNK signaling pathway, decreasing its stability and promoting prostate cancer cell proliferation. Ubiquitination assay, Western blot for p21 stability, pathway inhibitor treatment, HJURP overexpression and knockdown with proliferation readouts in vitro and in vivo Cell death & disease Medium 34099634
2024 HJURP is recruited to DNA double-strand break (DSB) sites through a mechanism requiring chromatin PARylation. At DSBs, HJURP promotes turnover of H3K9me3 and HP1, facilitating DNA damage signaling and DSB repair. HJURP overexpression also reorganizes global heterochromatin structure and increases radioresistance in glioma cells. Laser micro-irradiation to induce DSBs, HJURP-GFP recruitment imaging, PARP inhibitor and PARylation dependency assays, ChIP for H3K9me3 and HP1 at DSBs, comet assay, clonogenic survival after radiation Oncogene Medium 38279062
2024 HJURP forms disulfide-linked intermediates with PRDX1 through Cys327 and Cys457 residues, promoting PRDX1 redox cycling and inhibiting its hyperoxidation. This interaction enhances PRDX1 peroxidase activity, decreasing ROS levels and suppressing ferroptosis-inducer-induced lipid peroxidation in prostate cancer cells. Co-IP, disulfide crosslinking assays, cysteine mutagenesis (Cys327 and Cys457), in vitro peroxidase activity assay, ROS and lipid peroxidation measurements, in vitro and in vivo ferroptosis assays Redox biology High 39405980
2022 HJURP affects ubiquitination of YAP1 protein, regulating its stability and downstream transcriptional activity in triple-negative breast cancer. YAP1 in turn positively regulates NDRG1 transcription by binding its promoter, and the HJURP/YAP1/NDRG1 axis affects cell proliferation and chemotherapy sensitivity. Co-IP of HJURP and YAP1, ubiquitination assay, promoter binding (ChIP/reporter), HJURP and YAP1 knockdown epistasis, proliferation and chemosensitivity assays Cell death & disease Medium 35459269
2023 NFE2L1 transcriptionally activates HJURP by binding to its promoter, as confirmed by dual luciferase reporter and chromatin immunoprecipitation assays. HJURP inhibition attenuates the proliferation and ferroptosis-suppressive effects of NFE2L1 overexpression in oral squamous cell carcinoma cells. Dual luciferase reporter assay, ChIP assay for NFE2L1 at HJURP promoter, HJURP knockdown epistasis in NFE2L1-overexpressing cells Journal of bioenergetics and biomembranes Medium 37848756
2025 HJURP directly binds the C-terminal domain of CENP-C in vitro, and this interaction is essential for new CENP-A incorporation in chicken DT40 cells. CENP-C and the Mis18 complex provide dual, parallel recruitment pathways for HJURP localization to centromeres; abolishing both pathways completely prevents HJURP centromere localization and CENP-A incorporation. CENP-C, HJURP, and Mis18C form a tight association in the chromatin fraction. In vitro binding assay (recombinant HJURP and CENP-C CTD), HJURP CENP-C-binding mutants in DT40 cells, Mis18C knockout combined with HJURP mutant, Co-IP of CENP-C/HJURP/Mis18C from chromatin fraction, immunofluorescence of CENP-A incorporation bioRxivpreprint Medium
2025 Under sustained replication stress, ATR promotes CENP-A eviction from centromeres by recruiting the AAA+ ATPase VCP to centromeres, destabilizing CENP-A–containing nucleosomes. HJURP (but not H3 chaperones DAXX or ATRX) is necessary for subsequent nucleolar relocalization of displaced CENP-A. Replication stress induction, ATR inhibitor treatment, VCP inhibitor/depletion, immunofluorescence of CENP-A localization, HJURP/DAXX/ATRX RNAi epistasis for nucleolar CENP-A bioRxivpreprint Low

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP. Cell 556 19410544
2009 HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres. Cell 528 19410545
2011 HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore. The Journal of cell biology 284 21768289
2010 Epigenetic engineering shows H3K4me2 is required for HJURP targeting and CENP-A assembly on a synthetic human kinetochore. The EMBO journal 246 21157429
2010 HJURP binds CENP-A via a highly conserved N-terminal domain and mediates its deposition at centromeres. Proceedings of the National Academy of Sciences of the United States of America 163 20080577
2011 Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes & development 153 21478274
2012 HJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly. Developmental cell 102 22406139
2011 Xenopus HJURP and condensin II are required for CENP-A assembly. The Journal of cell biology 94 21321101
2018 Inheritance of CENP-A Nucleosomes during DNA Replication Requires HJURP. Developmental cell 80 30293838
2014 Mitotic regulator Mis18β interacts with and specifies the centromeric assembly of molecular chaperone holliday junction recognition protein (HJURP). The Journal of biological chemistry 76 24519934
2014 Phosphorylation and DNA binding of HJURP determine its centromeric recruitment and function in CenH3(CENP-A) loading. Cell reports 76 25001279
2013 Dimerization of the CENP-A assembly factor HJURP is required for centromeric nucleosome deposition. The EMBO journal 63 23771058
2018 HJURP promotes hepatocellular carcinoma proliferation by destabilizing p21 via the MAPK/ERK1/2 and AKT/GSK3β signaling pathways. Journal of experimental & clinical cancer research : CR 60 30111352
2011 Misregulation of Scm3p/HJURP causes chromosome instability in Saccharomyces cerevisiae and human cells. PLoS genetics 58 21980305
2019 Mechanism of centromere recruitment of the CENP-A chaperone HJURP and its implications for centromere licensing. Nature communications 52 31492860
2018 HJURP antagonizes CENP-A mislocalization driven by the H3.3 chaperones HIRA and DAXX. PloS one 45 30365520
2013 Modulation of HJURP (Holliday Junction-Recognizing Protein) levels is correlated with glioblastoma cells survival. PloS one 42 23638004
2015 HJURP is involved in the expansion of centromeric chromatin. Molecular biology of the cell 39 26063729
2017 Silencing of HJURP induces dysregulation of cell cycle and ROS metabolism in bladder cancer cells via PPARγ-SIRT1 feedback loop. Journal of Cancer 36 28819432
2019 Knockdown of HJURP inhibits non-small cell lung cancer cell proliferation, migration, and invasion by repressing Wnt/β-catenin signaling. European review for medical and pharmacological sciences 34 31115012
2021 Super Enhancer-Mediated Upregulation of HJURP Promotes Growth and Survival of t(4;14)-Positive Multiple Myeloma. Cancer research 33 34893510
2021 HJURP promotes proliferation in prostate cancer cells through increasing CDKN1A degradation via the GSK3β/JNK signaling pathway. Cell death & disease 31 34099634
2016 HJURP interaction with the condensin II complex during G1 promotes CENP-A deposition. Molecular biology of the cell 30 27807043
2022 HJURP regulates cell proliferation and chemo-resistance via YAP1/NDRG1 transcriptional axis in triple-negative breast cancer. Cell death & disease 29 35459269
2019 CENP-A nucleosome clusters form rosette-like structures around HJURP during G1. Nature communications 26 31570711
2019 HJURP Promotes Epithelial-to-Mesenchymal Transition via Upregulating SPHK1 in Hepatocellular Carcinoma. International journal of biological sciences 24 31223275
2013 HJURP regulates cellular senescence in human fibroblasts and endothelial cells via a p53-dependent pathway. The journals of gerontology. Series A, Biological sciences and medical sciences 23 23292286
2022 HJURP Promotes Malignant Progression and Mediates Sensitivity to Cisplatin and WEE1-inhibitor in Serous Ovarian Cancer. International journal of biological sciences 20 35173547
2024 HJURP inhibits sensitivity to ferroptosis inducers in prostate cancer cells by enhancing the peroxidase activity of PRDX1. Redox biology 19 39405980
2016 A Non-Synonymous Single Nucleotide Polymorphism in the HJURP Gene Associated with Susceptibility to Hepatocellular Carcinoma among Chinese. PloS one 18 26863619
2019 HJURP knockdown disrupts clonogenic capacity and increases radiation-induced cell death of glioblastoma cells. Cancer gene therapy 17 31138900
2020 The ATAD2/ANCCA homolog Yta7 cooperates with Scm3HJURP to deposit Cse4CENP-A at the centromere in yeast. Proceedings of the National Academy of Sciences of the United States of America 16 32079723
2023 Repression of CENP-A assembly in metaphase requires HJURP phosphorylation and inhibition by M18BP1. The Journal of cell biology 15 37141119
2023 NFE2L1 restrains ferroptosis by transcriptionally regulating HJURP and participates in the progress of oral squamous cell carcinoma. Journal of bioenergetics and biomembranes 12 37848756
2023 Advances in holliday junction recognition protein (HJURP): Structure, molecular functions, and roles in cancer. Frontiers in cell and developmental biology 11 37025176
2024 HJURP is recruited to double-strand break sites and facilitates DNA repair by promoting chromatin reorganization. Oncogene 9 38279062
2020 Essentiality of CENP-A Depends on Its Binding Mode to HJURP. Cell reports 9 33207191
2007 Identification of FAKTS as a novel 14-3-3-associated nuclear protein. Proteins 9 17256767
2024 HJURP Derived from Cancer-Associated Fibroblasts Promotes Glutamine Metabolism to Induce Resistance to Doxorubicin in Ovarian Cancer. The Tohoku journal of experimental medicine 6 38866531
2022 HJURP inhibits proliferation of ovarian cancer cells by regulating CENP-A/CENP-N. Bulletin du cancer 6 35940943
2022 Unraveling the Role of Histone Variant CENP-A and Chaperone HJURP Expression in Thymic Epithelial Neoplasms. International journal of molecular sciences 5 35955489
2025 HJURP modulates cell proliferation and chemoresistance via the MYC/TOP2A transcriptional axis in gastric cancer. Frontiers in molecular biosciences 4 40290723
2024 Oncogenic HJURP enhancer promotes the aggressive behavior of triple-negative breast cancer in association with p53/E2F1/FOXM1-axis. Cancer letters 3 39736453
2022 Pan-cancer analysis based on epigenetic modification explains the value of HJURP in the tumor microenvironment. Scientific reports 3 36460821
2024 The Impact of DAXX, HJURP and CENPA Expression in Uveal Melanoma Carcinogenesis and Associations with Clinicopathological Parameters. Biomedicines 2 39200236
2025 The multifaceted role of HJURP in cancer: Implications for tumorigenesis and therapeutic targeting. Gene 0 40902691
2024 Holliday junction recognition protein (HJURP) could reflect the clinical outcomes of lung adenocarcinoma patients, and impact the choice of precision therapy. Frontiers in genetics 0 39649097
2017 Construction and identification of a model for HJURP gene defect expression in human embryo villus cells. Clinical and experimental obstetrics & gynecology 0 29949288

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