Affinage

HJURP

Holliday junction recognition protein · UniProt Q8NCD3

Length
748 aa
Mass
83.5 kDa
Annotated
2026-04-28
48 papers in source corpus 29 papers cited in narrative 29 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HJURP is the dedicated histone chaperone for the centromere-specific histone H3 variant CENP-A, essential for both de novo CENP-A deposition in early G1 and inheritance of CENP-A nucleosomes during S-phase DNA replication. Its conserved N-terminal CENP-A binding domain (CBD) recognizes the CATD of CENP-A/H4 heterodimers with high specificity, capping the DNA-binding surface to prevent premature nucleosome formation, while its C-terminal dimerization domain enables assembly of octameric CENP-A nucleosomes (PMID:19410544, PMID:21478274, PMID:23771058). HJURP is recruited to centromeres through dual pathways involving the Mis18 complex (Mis18α/β and M18BP1) and CENP-C, with CDK-dependent phosphorylation restricting centromeric access to telophase/G1 by blocking the HJURP–CENP-C interaction (PMID:24519934, PMID:37141119, PMID:31492860); during S phase, HJURP cooperates with the MCM2-7 helicase to recycle parental CENP-A nucleosomes through replication forks (PMID:30293838). Beyond centromere biology, HJURP is recruited to DNA double-strand breaks via PARylation-dependent mechanisms to promote heterochromatin remodeling and DSB repair, and forms disulfide-linked intermediates with PRDX1 to enhance peroxidase activity and suppress ferroptosis (PMID:38279062, PMID:39405980).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2007 Medium

    Before its centromeric role was known, the initial characterization established that HJURP is a nuclear protein whose interaction with 14-3-3 proteins is regulated by Akt/PKB-dependent phosphorylation at Ser479, hinting at signaling-responsive regulation.

    Evidence Yeast two-hybrid, co-IP, site-directed mutagenesis of S479A in mammalian cells

    PMID:17256767

    Open questions at the time
    • Functional consequence of 14-3-3 binding for HJURP activity unknown
    • Relationship to centromere function not yet recognized
  2. 2009 High

    Two simultaneous studies resolved the long-standing question of how new CENP-A is deposited at centromeres after replication, establishing HJURP as the dedicated CENP-A chaperone that forms a prenucleosomal complex with CENP-A/H4 and is required for G1-phase CENP-A loading via recognition of the CATD.

    Evidence Co-IP, mass spectrometry, RNAi with CENP-A localization readout, cell-cycle fractionation, live-cell imaging in two independent labs

    PMID:19410544 PMID:19410545

    Open questions at the time
    • Structural basis of CENP-A recognition not yet determined
    • Mechanism of centromeric recruitment unknown
  3. 2010 High

    In vitro reconstitution demonstrated that HJURP directly and stoichiometrically binds CENP-A/H4 (but not H3/H4) through a conserved N-terminal CBD containing a TLTY motif, and can deposit CENP-A/H4 onto naked DNA, establishing its intrinsic chaperone activity independent of other centromere factors.

    Evidence Bacterially expressed protein binding assays, in vitro chromatin assembly, TLTY box mutagenesis

    PMID:20080577

    Open questions at the time
    • Atomic-resolution structure of the HJURP–CENP-A–H4 complex not yet available
    • Epigenetic requirements for centromeric targeting not addressed
  4. 2010 High

    The discovery that H3K4me2 at centromeric chromatin is required for HJURP recruitment revealed an upstream epigenetic prerequisite for CENP-A deposition, linking histone modification state to chaperone access.

    Evidence LSD1 demethylase tethering to human artificial chromosome, ChIP, CENP-A incorporation assay

    PMID:21157429

    Open questions at the time
    • Direct mechanism by which H3K4me2 promotes HJURP binding unknown
    • Whether HJURP reads the mark directly or via an intermediary unclear
  5. 2011 High

    The crystal structure of the HJURP–CENP-A–H4 ternary complex resolved how HJURP achieves specificity: it binds a CENP-A/H4 heterodimer (not tetramer), with its C-terminal β-sheet capping the DNA-binding region to prevent premature nucleosome formation, and contacts a CENP-A surface distinct from canonical H3.

    Evidence X-ray crystallography with structure–function mutagenesis

    PMID:21478274

    Open questions at the time
    • How the heterodimer-bound state transitions to octameric nucleosome not explained
    • In vivo validation of specific structural contacts limited
  6. 2011 High

    Ectopic targeting of HJURP to a non-centromeric locus was sufficient to build a functional de novo centromere with full kinetochore assembly and microtubule attachment, proving HJURP is the rate-limiting activity for centromere specification; recruitment required the Mis18 complex, identifying the upstream licensing step.

    Evidence LacI/LacO ectopic targeting, in vitro nucleosome assembly, kinetochore-microtubule attachment assay, RNAi epistasis

    PMID:21768289

    Open questions at the time
    • Direct binding interface between HJURP and Mis18 components not mapped
    • Mechanism by which Mis18 licenses HJURP centromeric access unknown
  7. 2011 High

    Conservation of the HJURP/Scm3 mechanism was established: Xenopus HJURP is functionally interchangeable with human HJURP in egg extracts, and condensin II (but not condensin I) was identified as a required cofactor for CENP-A retention.

    Evidence Xenopus egg extract immunodepletion and complementation, condensin I/II selective depletion

    PMID:21321101

    Open questions at the time
    • Direct physical interaction between HJURP and condensin II not demonstrated
  8. 2012 High

    Systematic mutagenesis of CENP-A dissected the HJURP recognition code: surface-exposed CATD residues drive HJURP binding specificity, while buried CATD residues enforce rigidity needed for chromatin incorporation, and an intact CENP-A/CENP-A dimerization interface is required for stable nucleosome assembly after HJURP-mediated deposition.

    Evidence Surface and buried residue mutagenesis of CENP-A, in vitro binding and chromatin incorporation assays

    PMID:22406139

    Open questions at the time
    • How HJURP releases CENP-A during the deposition step not resolved
  9. 2013 High

    The discovery that HJURP homodimerizes through its C-terminal domain solved the heterodimer-to-octamer paradox: since each HJURP monomer binds one CENP-A/H4 dimer, dimerization brings two CENP-A/H4 dimers together for nucleosome assembly; dimerization is required for deposition but dispensable for centromere recruitment or CENP-A binding.

    Evidence Crystallography of the C-terminal dimerization domain, separation-of-function mutations, CENP-A deposition assay

    PMID:23771058

    Open questions at the time
    • Kinetics and directionality of the HJURP dimer-mediated assembly reaction in vivo not characterized
  10. 2014 High

    CDK-dependent phosphorylation was established as the temporal gating mechanism: phosphorylated HJURP cannot bind Mis18β, restricting centromere recruitment to the post-mitotic window; a non-phosphorylatable HJURP mutant loads CENP-A prematurely in S/G2 phase. HJURP also contains a DNA-binding domain required for CENP-A loading.

    Evidence Phosphomimetic and non-phosphorylatable mutants, co-IP mapping of HJURP-Mis18β interaction (residues 437–460), cell-cycle analysis

    PMID:24519934 PMID:25001279

    Open questions at the time
    • Whether CDK1 or CDK2 is the primary kinase in vivo debated
    • Structural basis of phosphorylation-dependent inhibition of Mis18β binding not resolved
  11. 2015 High

    Genetic dissection in DT40 cells mapped a separable HJURP–M18BP1 interaction domain and demonstrated that HJURP possesses a centromere expansion activity independent of its CENP-A binding function, revealing modular domain architecture.

    Evidence DT40 knockout with gene replacement, separation-of-function constructs, co-IP

    PMID:26063729

    Open questions at the time
    • Molecular mechanism of the centromere expansion activity unknown
  12. 2016 High

    HJURP was shown to directly bind condensin II (not condensin I) and recruit the CAPH2 subunit to centromeres in early G1, functionally linking condensin II-mediated chromatin remodeling to CENP-A deposition.

    Evidence Selective condensin I/II co-IP, CAPH2 localization, LacO chromatin decondensation assay, epistasis with condensin II depletion

    PMID:27807043

    Open questions at the time
    • Whether condensin II remodeling is catalytic or structural at centromeres unknown
    • Direct binding interface not mapped
  13. 2018 High

    A new S-phase role was uncovered: HJURP transiently associates with centromeres during replication and co-purifies with the MCM2-7 helicase, and is required for inheritance of pre-existing CENP-A nucleosomes through the replication fork, establishing a dual-phase function for the chaperone.

    Evidence BioID proximity labeling, co-purification with MCM2, RNAi during S phase with CENP-A inheritance readout

    PMID:30293838

    Open questions at the time
    • Whether HJURP directly binds MCM2 or acts through an intermediary not fully resolved
    • Stoichiometry and topology of the HJURP-MCM2-CENP-A complex unknown
  14. 2019 High

    Biochemical reconstitution of the full Mis18 complex with HJURP revealed that two HJURP repeats are functionally interchangeable and bind to a 4:2:2 Mis18α:Mis18β:M18BP1 complex; Mis18α N-terminal tails gate HJURP access to binding sites near the Mis18αβ C-terminal helices, defining the molecular licensing mechanism.

    Evidence Photo-cross-linking, size exclusion chromatography, site-directed mutagenesis of reconstituted complexes

    PMID:31492860

    Open questions at the time
    • How Mis18α autoinhibition is relieved in vivo not determined
    • Whether both HJURP binding sites are occupied simultaneously in cells unknown
  15. 2019 High

    Super-resolution imaging placed HJURP at the physical center of rosette-like CENP-A nucleosome clusters during G1, providing nanoscale spatial evidence that HJURP acts as the nucleation point for centromeric chromatin assembly.

    Evidence 2D/3D STORM/PALM super-resolution microscopy with quantitative co-localization

    PMID:31570711

    Open questions at the time
    • Dynamic assembly sequence not captured by fixed-cell imaging
  16. 2023 High

    A dual-lock timing model was established: CDK phosphorylation prevents the HJURP–CENP-C interaction in metaphase, while M18BP1.S competitively blocks HJURP access to CENP-C; removal of both inhibitory pathways causes ectopic CENP-A assembly in metaphase, revealing CENP-C as a direct centromeric receptor for HJURP.

    Evidence Cell-free Xenopus egg extract, non-phosphorylatable HJURP mutants, competitive inhibition assay with CENP-A deposition readout

    PMID:37141119

    Open questions at the time
    • Structural basis of HJURP–CENP-C interaction not yet resolved
    • Whether this mechanism is fully conserved in mammals not tested
  17. 2024 Medium

    An unexpected non-centromeric function was established: HJURP is recruited to DNA double-strand breaks through PARylation-dependent mechanisms, where it promotes turnover of H3K9me3 and HP1 to facilitate DSB repair and confer radioresistance.

    Evidence Immunofluorescence at laser-induced DSBs, PARP inhibition, H3K9me3/HP1 ChIP, HJURP overexpression/knockdown with DNA repair readout

    PMID:38279062

    Open questions at the time
    • Whether HJURP deposits CENP-A at DSBs or acts through a CENP-A-independent mechanism not resolved
    • PAR-binding domain of HJURP not identified
    • Single lab finding not yet independently replicated
  18. 2024 High

    A redox-regulatory function was discovered: HJURP forms disulfide-linked intermediates with PRDX1 through specific cysteine residues (C327, C457), promoting PRDX1 redox cycling, preventing hyperoxidation, and suppressing ferroptosis in prostate cancer cells.

    Evidence Disulfide bond trapping, cysteine mutagenesis, peroxidase activity assay, ROS measurement, ferroptosis assay in vitro and in vivo

    PMID:39405980

    Open questions at the time
    • Physiological context of HJURP-PRDX1 interaction beyond cancer unclear
    • Whether this function is connected to centromere biology or entirely independent unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the structural basis of the HJURP–CENP-C interaction, the mechanism by which HJURP coordinates with the MCM2-7 helicase during replication-coupled CENP-A recycling, whether the DSB repair and PRDX1 redox functions operate through CENP-A-dependent or -independent mechanisms, and how HJURP release from assembled CENP-A nucleosomes is triggered.
  • No high-resolution structure of HJURP–CENP-C complex
  • MCM2-HJURP-CENP-A ternary complex architecture undetermined
  • CENP-A dependence of DSB and redox roles not tested
  • HJURP nucleosome release mechanism unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0044183 protein folding chaperone 6 GO:0042393 histone binding 4 GO:0003677 DNA binding 1 GO:0016209 antioxidant activity 1
Localization
GO:0005694 chromosome 3 GO:0005634 nucleus 2 GO:0005829 cytosol 2
Pathway
R-HSA-4839726 Chromatin organization 5 R-HSA-1640170 Cell Cycle 4 R-HSA-69306 DNA Replication 1 R-HSA-73894 DNA Repair 1
Partners
CAPH2CENPACENPCHJURPMCM2MIS18BMIS18BP1PRDX1
Complex memberships
HJURP-CENP-A/H4 prenucleosomal complexMis18α/Mis18β/M18BP1-HJURP licensing complex

Evidence

Reading pass · 29 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; HJURP recognition of CENP-A is mediated through the centromere targeting domain (CATD) of CENP-A. Co-immunoprecipitation, mass spectrometry, RNAi knockdown with CENP-A localization readout, cell-cycle fractionation Cell High 19410544 19410545
2009 HJURP centromeric localization is cell-cycle regulated, transiently appearing at centromeres coinciding precisely with the window for new CENP-A deposition; HJURP downregulation causes major reduction of CENP-A at centromeres and mitotic defects. Immunofluorescence, live-cell imaging, RNAi knockdown, cell-cycle analysis Cell High 19410544 19410545
2010 Bacterially expressed HJURP binds the CENP-A/H4 tetramer but not the H3/H4 tetramer at a stoichiometric ratio through a conserved N-terminal domain (CBD) containing a TLTY box; HJURP facilitates deposition of CENP-A/H4 tetramers onto naked DNA in vitro. In vitro binding assay with bacterially expressed proteins, in vitro chromatin assembly assay, mutagenesis of TLTY box Proceedings of the National Academy of Sciences of the United States of America High 20080577
2010 H3K4me2 at the kinetochore is required for efficient HJURP recruitment and CENP-A incorporation; depletion of H3K4me2 via tethered LSD1 demethylase caused loss of HJURP recruitment and failure to incorporate new CENP-A, gradually inactivating the kinetochore. Epigenetic engineering (LSD1 tethering to HAC), ChIP, immunofluorescence, CENP-A incorporation assay The EMBO journal High 21157429
2011 LacI-HJURP fusion drives stable recruitment of CENP-A to a LacO array at a non-centromeric locus, sufficient to direct assembly of a functional de novo centromere with CCAN proteins, NDC80, and stable kinetochore-microtubule attachments; the HJURP N-terminal fragment assembles CENP-A nucleosomes in vitro; HJURP centromere recruitment requires the Mis18 complex. LacI/LacO ectopic targeting, in vitro nucleosome assembly, immunofluorescence, kinetochore-microtubule attachment assay, RNAi epistasis The Journal of cell biology High 21768289
2011 Crystal structure of the HJURP–CENP-A–H4 complex reveals that HJURP binds a CENP-A/H4 heterodimer; the C-terminal β-sheet domain of HJURP caps the DNA-binding region of the heterodimer, preventing spontaneous DNA association; a novel CENP-A surface site distinct from H3 mediates HJURP binding specificity. X-ray crystallography, structure–function mutagenesis Genes & development High 21478274
2011 Xenopus HJURP (xHJURP) is required for CENP-A deposition in a Xenopus egg extract system that recapitulates spatial and temporal specificity of human CENP-A deposition; human HJURP can substitute for xHJURP; condensin II (but not condensin I) is required for CENP-A assembly and retention of centromeric CENP-A nucleosomes. Xenopus egg extract in vitro system, immunodepletion, complementation with human HJURP, condensin I/II depletion The Journal of cell biology High 21321101
2011 Overexpression of HJURP causes chromosome loss and mitotic defects in human cells; in yeast, overexpression of Scm3 (HJURP ortholog) leads to premature separation of sister chromatids and reduction of Cse4p/H4 at centromeres; an N-terminal domain of Scm3 mediates centromeric DNA interaction and the chromosome loss phenotype. Overexpression in human cells and yeast, chromosome loss assay, ChIP, mutant allele analysis, genetic suppression PLoS genetics High 21980305
2012 Surface-exposed CATD residues of CENP-A are primary determinants for HJURP recognition, while buried CATD residues generating rigidity with H4 are required for efficient centromeric incorporation; HJURP contact points adjacent to CATD on CENP-A are used not for binding specificity but to transmit stability through histone fold domains of CENP-A and H4; an intact CENP-A/CENP-A interface is required for stable chromatin incorporation upon HJURP-mediated assembly. Mutagenesis of CENP-A surface/buried residues, in vitro binding assays, CENP-A incorporation assay 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 preassembly complex and at chromatin during new CENP-A deposition; dimerization is essential for deposition of new CENP-A nucleosomes but not for HJURP recruitment to centromeres or CENP-A binding. Crystallography and biochemical assays for dimerization, separation-of-function mutations, CENP-A deposition assay The EMBO journal High 23771058
2013 HJURP plays a role in regulating cellular senescence through a p53-dependent pathway; HJURP knockdown in young human fibroblasts and endothelial cells leads to premature senescence that is rescued by p53 knockdown but not p16 knockdown. RNAi knockdown, senescence assays, epistasis with p53/p16 knockdown The journals of gerontology. Series A, Biological sciences and medical sciences Medium 23292286
2014 HJURP directly binds Mis18β through a minimal region mapped to residues 437–460; Mis18β depletion dramatically impairs HJURP recruitment to centromeres; CDK1 phosphorylation of HJURP weakens its interaction with Mis18β, providing temporal regulation of CENP-A deposition after mitosis. Co-IP, mapping of binding domain, RNAi, phosphomimetic/non-phosphorylatable mutants The Journal of biological chemistry High 24519934
2014 Cell-cycle-dependent phosphorylation of HJURP by cyclin-dependent kinases controls its centromeric recruitment; a non-phosphorylatable HJURP mutant localizes prematurely to centromeres in S and G2 phase, causing premature CENP-A loading and cell-cycle delays; HJURP also possesses a DNA-binding domain required mechanistically for CenH3(CENP-A) loading. Phosphomimetic/non-phosphorylatable HJURP mutants, cell-cycle analysis, CENP-A deposition assay, DNA-binding domain mutagenesis Cell reports High 25001279
2015 The middle region of HJURP associates with the Mis18 complex protein M18BP1/KNL2, and this HJURP–M18BP1 association is required for HJURP function in centromere formation; HJURP also possesses a centromere expansion activity separable from its CENP-A-binding activity. DT40 knockout cell lines, gene replacement constructs, co-IP, ectopic HJURP targeting assay Molecular biology of the cell High 26063729
2016 HJURP selectively associates with condensin II (not condensin I) and recruits CAPH2 (condensin II subunit) to early G1 centromeres; condensin II function at the centromere, dependent on HJURP, is required for new CENP-A deposition; HJURP induces decondensation of non-centromeric chromatin that is modulated by condensin II. Co-IP (selective condensin I/II pulldown), CAPH2 localization assay, LacO decondensation assay, condensin II depletion with CENP-A deposition readout Molecular biology of the cell High 27807043
2018 HJURP transiently associates with centromeres during S phase and binds to pre-existing CENP-A; HJURP is required for centromeric nucleosome inheritance during S phase; HJURP co-purifies with the MCM2-7 helicase complex and, together with MCM2 subunit, simultaneously binds CENP-A. BioID proximity labeling, co-purification, RNAi knockdown during S phase, CENP-A inheritance assay Developmental cell High 30293838
2018 HJURP destabilizes p21 via the MAPK/ERK1/2 and AKT/GSK3β pathways, which regulate nucleus-cytoplasm translocation and ubiquitin-mediated degradation of p21, promoting hepatocellular carcinoma cell proliferation. Co-IP, Western blot, pharmacological inhibitors (U0126, SC-79), RNAi, p21 knockdown rescue Journal of experimental & clinical cancer research : CR Medium 30111352
2018 HJURP antagonizes ectopic CENP-A deposition driven by H3.3 chaperones HIRA and DAXX; the balance between HJURP levels and CENP-A is essential to prevent ectopic CENP-A assembly by H3.3 chaperones. RNAi knockdown/overexpression, ChIP, immunofluorescence in human cancer cells PloS one Medium 30365520
2019 Two repeats in human HJURP proposed to be functionally distinct are interchangeable and bind concomitantly to the 4:2:2 Mis18α:Mis18β:M18BP1 complex without dissociating it; the Mis18α N-terminal tails block two identical HJURP-repeat binding sites near Mis18αβ C-terminal helices, identified by photo-cross-linking; HJURP binds CENP-A:H4 dimers, implying tetramer assembly requires two Mis18αβ:M18BP1:HJURP complexes or consecutive rounds. Biochemical reconstitution, photo-cross-linking, site-directed mutagenesis, size exclusion chromatography Nature communications High 31492860
2019 Super-resolution microscopy reveals that CENP-A nucleosomes form rosette-like clusters (~250–300 nm) during G1 with HJURP located at the center, serving as a nucleation point for CENP-A deposition. 2D and 3D super-resolution microscopy (STORM/PALM), co-localization analysis, segmentation analysis Nature communications High 31570711
2020 The CENP-A-HJURP binding interface differs between chicken and human, with W53 of HJURP being an essential contact for chicken CENP-A A59; two arginine residues introduced to the chicken HJURP αA-helix suppress mis-incorporation caused by CENP-A A59Q mutation, explaining species-specific binding affinity. In vivo mutagenesis in chicken DT40 cells, CENP-A incorporation assay, binding affinity measurements Cell reports High 33207191
2021 HJURP increases ubiquitination of CDKN1A (p21) via the GSK3β/JNK signaling pathway, decreasing p21 stability and promoting prostate cancer cell proliferation. Co-IP, ubiquitination assay, Western blot, RNAi, overexpression, in vivo xenograft Cell death & disease Medium 34099634
2022 HJURP affects ubiquitination of YAP1 protein, regulating its stability and downstream transcriptional activity; YAP1 in turn positively regulates NDRG1 transcription by binding its promoter, establishing an HJURP/YAP1/NDRG1 axis in triple-negative breast cancer. Co-IP, ubiquitination assay, promoter binding assay, RNAi, overexpression Cell death & disease Medium 35459269
2023 HJURP phosphorylation prevents interaction between HJURP and CENP-C in metaphase, blocking delivery of soluble CENP-A to centromeres; M18BP1.S competitively inhibits HJURP access to CENP-C at centromeres; removal of both inhibitory activities causes CENP-A assembly in metaphase. Cell-free X. laevis egg extract centromere assembly system, non-phosphorylatable HJURP mutants, competitive inhibition assay, CENP-A deposition readout The Journal of cell biology High 37141119
2024 HJURP is recruited to DNA double-strand breaks (DSBs) via a mechanism requiring chromatin PARylation; at DSBs, HJURP promotes turnover of H3K9me3 and HP1, facilitating DNA damage signaling and DSB repair; HJURP overexpression globally alters heterochromatin structure and increases radioresistance. Immunofluorescence at DSB sites, PARP inhibition, H3K9me3/HP1 ChIP, HJURP overexpression/knockdown with DNA repair readout Oncogene Medium 38279062
2024 HJURP forms disulfide-linked intermediates with PRDX1 through Cys327 and Cys457 residues, promoting PRDX1 redox cycling, inhibiting PRDX1 hyperoxidation, enhancing PRDX1 peroxidase activity, reducing ROS levels, and suppressing ferroptosis in prostate cancer cells. Co-IP, disulfide bond trapping, cysteine mutagenesis, peroxidase activity assay, ROS measurement, ferroptosis assay in vitro and in vivo Redox biology High 39405980
2007 HJURP (then called clone 546/FAKTS) localizes to the nucleus of mammalian cells and interacts with 14-3-3 proteins in a manner enhanced by activated Akt/PKB; Ser479 is the predominant residue mediating this interaction, and AKT/PKB phosphorylates this site. Yeast two-hybrid, confocal microscopy, co-IP in mammalian cells, site-directed mutagenesis (S479A), Akt expression Proteins Medium 17256767
2025 HJURP directly binds to the C-terminal domain of CENP-C in vitro; this interaction is essential for new CENP-A incorporation; CENP-C and Mis18 complex provide dual recruitment pathways for HJURP at centromeres, and CENP-C, HJURP, and Mis18C form a tight association in the chromatin fraction. In vitro binding assay, Mis18 complex KO cells with HJURP CENP-C-binding mutant, co-IP from chromatin fraction in DT40 cells bioRxivpreprint Medium bio_10.1101_2025.10.05.680587
2025 Under replication stress, ATR promotes CENP-A eviction from centromeres by recruiting VCP (AAA+ ATPase) to destabilize CENP-A nucleosomes; HJURP (but not DAXX or ATRX) is required for nucleolar relocalization of displaced CENP-A. Replication stress induction, ATR inhibition, VCP depletion, HJURP/DAXX/ATRX knockdown, immunofluorescence for CENP-A localization bioRxivpreprint Medium bio_10.1101_2025.10.20.683416

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 553 19410544
2009 HJURP is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres. Cell 524 19410545
2011 HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore. The Journal of cell biology 280 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 162 20080577
2011 Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes & development 151 21478274
2012 HJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly. Developmental cell 101 22406139
2011 Xenopus HJURP and condensin II are required for CENP-A assembly. The Journal of cell biology 93 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 75 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 57 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 37 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 33 31115012
2021 Super Enhancer-Mediated Upregulation of HJURP Promotes Growth and Survival of t(4;14)-Positive Multiple Myeloma. Cancer research 32 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 25 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 22 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 18 39405980
2019 HJURP knockdown disrupts clonogenic capacity and increases radiation-induced cell death of glioblastoma cells. Cancer gene therapy 17 31138900
2016 A Non-Synonymous Single Nucleotide Polymorphism in the HJURP Gene Associated with Susceptibility to Hepatocellular Carcinoma among Chinese. PloS one 17 26863619
2023 Repression of CENP-A assembly in metaphase requires HJURP phosphorylation and inhibition by M18BP1. The Journal of cell biology 15 37141119
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 13 32079723
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 10 37025176
2024 HJURP is recruited to double-strand break sites and facilitates DNA repair by promoting chromatin reorganization. Oncogene 9 38279062
2007 Identification of FAKTS as a novel 14-3-3-associated nuclear protein. Proteins 9 17256767
2020 Essentiality of CENP-A Depends on Its Binding Mode to HJURP. Cell reports 8 33207191
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
2025 HJURP modulates cell proliferation and chemoresistance via the MYC/TOP2A transcriptional axis in gastric cancer. Frontiers in molecular biosciences 3 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 Unraveling the Role of Histone Variant CENP-A and Chaperone HJURP Expression in Thymic Epithelial Neoplasms. International journal of molecular sciences 3 35955489
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