Affinage

NAP1L1

Nucleosome assembly protein 1-like 1 · UniProt P55209

Round 2 corrected
Length
391 aa
Mass
45.4 kDa
Annotated
2026-04-29
130 papers in source corpus 32 papers cited in narrative 32 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NAP1L1 is a histone chaperone that facilitates nucleosome assembly and disassembly by binding H2A-H2B and H3-H4 with nanomolar affinity, shielding histone interaction surfaces from nonproductive DNA contacts and lowering the thermodynamic barrier to nucleosome formation in a two-step process (PMID:18728017, PMID:20347425, PMID:23973327, PMID:23050009). Beyond canonical nucleosome assembly, NAP1L1 evicts linker histone H1 through recruitment by activator-bound p300 to enable gene-specific transcription (PMID:30902546), enhances CSB-mediated nucleosome remodeling during transcription-coupled DNA repair (PMID:28369616), stimulates RAD54/RAD51-dependent homologous recombination by evicting H1 from higher-order chromatin at double-strand breaks (PMID:24798879), and controls cohesin release during mitosis by antagonizing PP2A-mediated dephosphorylation of the cohesin subunit SA (PMID:24086141). CK2 phosphorylation promotes its nuclear import for S-phase functions (PMID:18086883), and glutamylation regulates its control of linker histone dynamics on mitotic chromosomes (PMID:25897082). In mammalian cells, NAP1L1 maintains neural progenitor proliferation via SETD1A-mediated H3K4me3 at the RassF10 promoter (PMID:29490266) and promotes tumor cell proliferation through epigenetic silencing of the CDKN1C/p57 tumor suppressor (PMID:25071868) and activation of a HDGF/c-Jun/CCND1 signaling axis (PMID:34959221, PMID:35351053).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1995 High

    Establishing that NAP1 functions in mitotic progression beyond histone chaperoning resolved the question of whether NAP1 acts solely as a nucleosome assembly factor, revealing it is required for cyclin Clb2-dependent mitotic functions including spindle elongation and bud morphogenesis.

    Evidence NAP1 deletion in S. cerevisiae combined with Clb2 functional assays and cell-cycle phenotyping

    PMID:7622567

    Open questions at the time
    • Mechanism by which NAP1 enables Clb2 mitotic functions was unclear
    • No direct binding between NAP1 and Clb2/CDC28 demonstrated
  2. 1997 High

    Discovery that NAP1 physically associates with the kinase Gin4 and together with Clb2 activates Gin4 phosphorylation established NAP1 as a scaffold linking cyclin-CDK complexes to downstream mitotic kinase cascades.

    Evidence Affinity chromatography, in vivo phosphorylation and kinase assays, genetic epistasis in S. cerevisiae

    PMID:9214386

    Open questions at the time
    • Whether NAP1 serves as a kinase substrate or purely as a scaffold was unresolved
    • Relevance to mammalian NAP1L1 not tested
  3. 2003 High

    Demonstration that NAP1 deletion causes genome-wide transcriptional changes clustered along chromosomes, combined with the finding that NAP1 shuttles between cytoplasm and nucleus via a functional NES required for mitotic function, established that nucleocytoplasmic trafficking is essential for NAP1's chromatin-regulatory role.

    Evidence Microarray profiling of Δnap1 yeast; GFP localization, NES mutagenesis, and complementation assays in S. cerevisiae

    PMID:12788058 PMID:12944491

    Open questions at the time
    • Whether the transcriptional changes reflect direct nucleosome assembly defects or indirect effects was unknown
    • Nuclear import mechanism not yet identified
  4. 2007 High

    Three advances defined NAP1's biochemical mechanism: CK2 phosphorylation at three serines promotes nuclear import and S-phase progression; NAP1 modulates H3/H4 tetramer-dimer equilibrium to alter DNA supercoiling topology; and the corepressor Alien enhances NAP1-mediated nucleosome assembly at specific promoters.

    Evidence MS-based phosphosite mapping with CK2 kinase assays and mutagenesis in yeast; DNA supercoiling and crosslinking assays in vitro; co-IP, GST pulldown, ChIP, and nucleosome assembly assays

    PMID:17339334 PMID:17595058 PMID:18086883

    Open questions at the time
    • How CK2-phosphorylated NAP1 is recognized by the nuclear import machinery was unknown
    • Whether H3/H4 tetramer-dimer modulation occurs in vivo was untested
  5. 2008 High

    Quantitative measurement of NAP1-histone binding affinities (low nM for both H2A-H2B and H3-H4, two histone fold dimers per NAP1 dimer) established the thermodynamic framework explaining how histones transfer from chaperone to DNA during nucleosome assembly.

    Evidence Quantitative fluorescence-based binding assays with purified yeast Nap1 and histone complexes

    PMID:18728017

    Open questions at the time
    • Binding affinities for human NAP1L1 not measured
    • Kinetic rates of histone transfer not determined
  6. 2009 High

    Two studies expanded NAP1's functional repertoire: in Drosophila, NAP1 links the RLAF silencing complex to Notch-target genes by directing high nucleosome density and coordinating H3 deacetylation/H3K4me3 demethylation; in yeast, NAP1 forms a RanGTP-insensitive import complex with the histone variant Htz1/H2B and karyopherin Kap114 for Htz1 nuclear import.

    Evidence Proteomics, co-IP, ChIP, nucleosome density analysis in Drosophila; copurification and nuclear import assays with RanGTP competition in S. cerevisiae

    PMID:19782028 PMID:19929865

    Open questions at the time
    • Whether RLAF-NAP1 interaction occurs in mammalian cells was unknown
    • How NAP1 discriminates Htz1 from canonical H2A was unclear
  7. 2010 High

    Thermodynamic reconstitution proved that NAP1 promotes nucleosome assembly not by actively depositing histones but by eliminating competing nonnucleosomal histone-DNA complexes, lowering the free energy barrier to correct nucleosome formation.

    Evidence FRET, sedimentation, MNase assays in Δnap1 yeast, and transcription reporters

    PMID:20347425

    Open questions at the time
    • Whether other chaperones share this thermodynamic mechanism was not tested
    • Contribution of individual histone pairs to the energy barrier was unresolved
  8. 2011 High

    Structural studies using PELDOR spectroscopy resolved a long-standing question by showing NAP1-family chaperones bind H3-H4 as a tetramer (not dimers), and this tetrameric substrate can be used for nucleosome assembly and chaperone-mediated acetylation.

    Evidence Pulsed electron double resonance, protein crosslinking, in vitro nucleosome assembly and acetylation assays

    PMID:21329878

    Open questions at the time
    • Full structural model of NAP1-H3/H4 tetramer complex not available
    • Whether tetramer vs. dimer mode is regulated in vivo was unknown
  9. 2012 High

    Single-molecule magnetic tweezers revealed nucleosome assembly by NAP1 proceeds in two kinetic steps—initial DNA compaction followed by canonical nucleosome formation with a characteristic linking number change—providing a real-time mechanistic framework.

    Evidence Single-molecule magnetic tweezers measuring DNA extension and linking number

    PMID:23050009

    Open questions at the time
    • Whether the two-step pathway applies to all histone variants was untested
    • Rate-limiting step not identified
  10. 2013 High

    Three discoveries in 2013 deepened understanding of NAP1's histone-shielding, mitotic, and transcription-elongation functions: HDX-MS showed NAP1 shields H2A-H2B interaction surfaces and organizes two H2A-H2B copies into a pseudo-tetramer; in Drosophila, NAP1 controls mitotic cohesin release by displacing PP2A from cohesin in a cell-cycle-regulated manner; and in yeast, NAP1 modulates Rtt109-dependent H3K9 acetylation during transcription elongation to suppress cryptic transcription.

    Evidence HDX-MS with mutagenesis and in vivo validation; proteomics, co-IP, ChIP-seq, and genetic rescue in Drosophila; genetic suppression and ChIP in S. cerevisiae

    PMID:23401858 PMID:23973327 PMID:24086141

    Open questions at the time
    • Structural basis of NAP1-PP2A antagonism on cohesin was unknown
    • Whether NAP1's elongation role is conserved in mammals was untested
  11. 2014 High

    Two studies demonstrated direct roles in mammalian DNA repair and tumor biology: NAP1L1 accumulates at DSB sites, binds RAD54, and enhances homologous recombination by evicting H1 from higher-order chromatin; separately, NAP1L1 binds the CDKN1C/p57 promoter and promotes its methylation-mediated silencing, driving pancreatic neuroendocrine tumor proliferation.

    Evidence ChIP at DSBs, siRNA knockdown repair assay, in vitro RAD51/RAD54 HR reconstitution; ChIP of NAP1L1 at CDKN1C promoter, bisulfite methylation, orthotopic tumor model

    PMID:24798879 PMID:25071868

    Open questions at the time
    • Which DNA methyltransferase NAP1L1 recruits to CDKN1C was unknown
    • Whether NAP1L1's HR function requires its histone chaperone activity or is a distinct activity was unresolved
  12. 2015 High

    Discovery that glutamylation of NAP1 is required for linker histone H1 dynamics and mitotic chromosome condensation in Xenopus established post-translational charge modification as a regulatory switch controlling NAP1's histone chaperone activity.

    Evidence Immunodepletion and add-back of wild-type vs. glutamylation-mutant Nap1 in Xenopus egg extracts, FRAP, chromosome condensation assays

    PMID:25897082

    Open questions at the time
    • Identity of the glutamylase and deglutamylase acting on NAP1L1 was unknown
    • Whether glutamylation regulates NAP1 in interphase was not addressed
  13. 2017 High

    Single-molecule FRET studies showed NAP1L1 enhances CSB chromatin remodeling by suppressing non-productive DNA binding and reducing remodeler pausing, establishing NAP1L1 as a cofactor for transcription-coupled nucleotide excision repair; separately, HCV NS5A was shown to sequester NAP1L1 in the cytoplasm (and degrade it in genotype 2), impairing IRF3/TBK1 antiviral signaling.

    Evidence smFRET and TIRF microscopy with purified NAP1L1/CSB; co-IP, domain mapping, subcellular fractionation, siRNA knockdown with pathway readouts in hepatoma cells

    PMID:28369616 PMID:28659470

    Open questions at the time
    • Whether NAP1L1 enhances other chromatin remodelers besides CSB was untested
    • Mechanism by which NAP1L1 loss reduces RELA levels was unclear
  14. 2018 High

    NAP1L1's developmental and oncogenic roles were elaborated: in cortical development, NAP1L1 maintains neural progenitor proliferation by promoting SETD1A-dependent H3K4me3 at the RassF10 promoter; in cancer, NAP1L1 activates PI3K/AKT/mTOR signaling and participates in a KRAS/P-ERK/ETS1 positive feedback loop.

    Evidence CRISPR-KO mice, in utero electroporation, ChIP for H3K4me3, RassF10 rescue; luciferase 3'UTR assays, ChIP for ETS1, Western blotting in RCC and HCC cells

    PMID:29490266 PMID:29572888 PMID:30082686

    Open questions at the time
    • Direct physical interaction between NAP1L1 and SETD1A was not demonstrated
    • How NAP1L1 activates PI3K/AKT/mTOR at the biochemical level remains unknown
  15. 2019 High

    Two conceptual advances: in vitro chromatin reconstitution showed NAP1 is recruited by activator-bound p300 to evict linker histone H1 and enable gene-specific transcription (validated at the CD40 locus in B cells); separately, yeast Nap1 was shown to serve as a dedicated ribosomal protein chaperone for Rps6, extending its chaperone repertoire beyond histones.

    Evidence In vitro chromatin transcription system, co-IP of NAP1 with p300, B cell CD40 induction; TAP screen, in vitro solubility assay, genetic interaction in yeast

    PMID:30902546 PMID:31062022

    Open questions at the time
    • Whether Rps6 chaperoning is conserved in mammalian NAP1L1 was not tested
    • The structural basis of NAP1-p300 interaction was unknown
  16. 2021 Medium

    Independent studies in glioma and ovarian cancer identified a NAP1L1→HDGF→c-Jun→CCND1/CDK4/CDK6 proliferative axis, with co-IP confirming direct NAP1L1-HDGF interaction and HDGF rescue reversing NAP1L1 knockdown effects, establishing a non-chromatin oncogenic signaling role.

    Evidence Co-IP, immunofluorescence co-localization, siRNA knockdown, HDGF rescue, in vivo tumor model in glioma (2021) and ovarian cancer (2022) cells

    PMID:34959221 PMID:35351053

    Open questions at the time
    • Whether NAP1L1-HDGF interaction requires NAP1L1's histone-binding domain was untested
    • Direct mechanism linking NAP1L1 to HDGF activation of c-Jun is unclear
    • Findings from cancer cell lines without genetic validation

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major open questions include: the structural basis of NAP1L1 interactions with non-histone partners (p300, CSB, HDGF, cohesin), the mechanism by which NAP1L1 directs DNA methyltransferase activity to the CDKN1C promoter, whether its ribosomal protein chaperone function is conserved in mammals, and how post-translational modifications (CK2 phosphorylation, glutamylation) are coordinated to partition NAP1L1 among its diverse nuclear and cytoplasmic functions.
  • No high-resolution structure of full-length NAP1L1 with any partner complex
  • Integration of chromatin vs. non-chromatin functions is unexplored
  • In vivo significance of many cancer-context findings requires genetic models

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0042393 histone binding 6 GO:0044183 protein folding chaperone 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005634 nucleus 5 GO:0005829 cytosol 3 GO:0005694 chromosome 2
Pathway
R-HSA-4839726 Chromatin organization 8 R-HSA-1640170 Cell Cycle 4 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-73894 DNA Repair 2
Partners
ALIENCSBGIN4HDGFKAP114P300RAD54
Complex memberships
RLAF complex

Evidence

Reading pass · 32 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 Yeast NAP1 (ortholog of NAP1L1) is required for the mitotic cyclin Clb2 to carry out its full range of mitotic functions; in NAP1-deleted cells, Clb2/CDC28 kinase activity rises normally yet cells undergo prolonged delay at the short spindle stage, fail to switch from polar to isotropic bud growth, and show aberrant microtubule dynamics, demonstrating that NAP1 acts downstream of or in parallel to cyclin-CDK activation. Genetic deletion of NAP1 combined with Clb2 functional assays and cell-cycle phenotype analysis in S. cerevisiae The Journal of cell biology High 7622567
1997 Yeast NAP1 (ortholog of NAP1L1) physically associates with the kinase Gin4; NAP1 and the mitotic cyclin Clb2 together are required for phosphorylation and activation of Gin4, placing NAP1 in a pathway that links cyclin-CDK complexes to Gin4-dependent control of bud morphogenesis and mitotic progression. Affinity chromatography, in vivo phosphorylation assays, kinase activity assays, genetic epistasis in S. cerevisiae The Journal of cell biology High 9214386
1998 NAP1L1 is a member of the TSPY-SET-NAP1L1 gene family; TSPYL genes were identified as novel members of this family by EST analysis and sequence homology, establishing the evolutionary relationships among NAP1L1, SET, and TSPY. EST sequence analysis, chromosomal localization, expression profiling Cytogenetics and cell genetics Low 9730615
2003 Deletion of yeast NAP1 (ortholog of NAP1L1) leads to genome-wide transcriptional changes (~10% of ORFs altered ≥2-fold) that are clustered along chromosomes, indicating NAP1 is required for maintenance of cumulative nucleosome formation in vivo and that loss of NAP1 disrupts local chromatin architecture. Genome-wide DNA microarray expression profiling of Δnap1 S. cerevisiae Biochemical and biophysical research communications Medium 12788058
2003 Yeast NAP1 (ortholog of NAP1L1) shuttles between cytoplasm and nucleus; a putative nuclear export signal (NES) in yNap1 mediates its cytoplasmic localization, and NES-deletion mutants accumulate in the nucleus. Nucleocytoplasmic shuttling is required for NAP1 function in mitotic progression, as NES-lacking mutants fail to complement mitotic delay and temperature-sensitive growth phenotypes of NAP1-deleted strains. GFP localization, NES mutagenesis, complementation of nap1 deletion phenotypes in S. cerevisiae Molecular and cellular biology High 12944491
2007 Yeast NAP1 (ortholog of NAP1L1) is phosphorylated in vivo at 11 sites; casein kinase 2 (CK2) phosphorylates three specific serine residues on NAP1. Phosphorylation of these serines by CK2 promotes nuclear import of NAP1 and is required for normal S-phase progression, as serine-to-alanine or serine-to-aspartate mutations both prolong S phase. Mass spectrometry identification of phosphorylation sites, in vitro CK2 kinase assays, alanine/aspartate mutagenesis, cell-cycle analysis in S. cerevisiae Molecular and cellular biology High 18086883
2007 The corepressor Alien binds NAP1 (ortholog of NAP1L1) in vivo and in vitro and enhances NAP1-mediated nucleosome assembly on DNA. Alien also reduces the accessibility of histones H3 and H4 for the NAP1-promoted assembly reaction, and both NAP1 and Alien localize to the endogenous CYP24 promoter, a VDR target gene, in vivo. Co-IP, GST pulldown, in vitro nucleosome assembly assay, chromatin immunoprecipitation and re-ChIP Molecular and cellular biology High 17339334
2007 Excess NAP1 (ortholog of NAP1L1) added to H3/H4 shifts the tetramer–dimer equilibrium toward dimers, and H3/H4 dimers deposited on DNA form positively supercoiled DNA, whereas tetramers form negatively supercoiled DNA. NAP1 can also alter the conformational state of pre-bound H3/H4, suggesting a role in modulating chromatin topology during transcription. DNA supercoiling assays, formaldehyde crosslinking, DTNB modification of H3-Cys110, topoisomerase-relaxation assays in vitro Biochemistry Medium 17595058
2008 Yeast NAP1 (ortholog of NAP1L1) binds H2A/H2B and H3/H4 histone complexes with low nanomolar affinity; each NAP1 dimer binds two histone fold dimers. The NAP1 tails contribute synergistically to histone binding, whereas histone tails have a slightly repressive effect. The (H3/H4)₂ tetramer binds DNA with higher affinity than it binds NAP1, establishing a thermodynamic framework for histone exchange. Quantitative fluorescence-based binding assays, thermodynamic analysis of purified yNap1 and histone complexes in vitro The Journal of biological chemistry High 18728017
2009 Drosophila NAP1 (ortholog of NAP1L1) interacts with the RLAF silencing complex (comprising RPD3, LID/KDM5, SIN3A, PF1, EMSY, MRG15) and links it to the Su(H)/Hairless DNA-binding complex at NOTCH-regulated E(spl) genes. NAP1 directs high nucleosome density near E(spl) control elements and mediates both H3 deacetylation and H3K4me3 demethylation by RLAF, distinguishing its function from that of ASF1. Proteomics/mass spectrometry interaction network, co-IP, ChIP, nucleosome density analysis in Drosophila Molecular cell High 19782028
2009 Yeast NAP1 (ortholog of NAP1L1) forms an RanGTP-insensitive import complex with Htz1/H2B and the karyopherin Kap114, facilitating nuclear import of the histone variant Htz1. NAP1 is required for maintaining a soluble cytoplasmic pool of Htz1, and NAP1 has Htz1-independent functions not shared by the chaperone Chz1. Copurification, nuclear import assays, RanGTP competition assays, genetic analysis in S. cerevisiae Traffic High 19929865
2009 HIV-1 Rev protein forms a stable complex with human nucleosome assembly protein 1 (Nap1, a NAP1L1-family member) through the Rev arginine-rich domain; Nap1 alters the oligomerization state of Rev in vitro. Overexpression of Nap1 stimulates Rev-mediated RNA export, reduces nucleolar localization of Rev, and affects Rev nuclear import rates. Tandem affinity purification (TAP), Rev affinity column retention, in vitro oligomerization assay, overexpression functional assays in human cells Virology Medium 19339032
2010 Yeast NAP1 (ortholog of NAP1L1) promotes nucleosome assembly by eliminating competing nonnucleosomal histone-DNA interactions; thermodynamic studies show NAP1 lowers the free energy barrier for nucleosome formation. Deletion of NAP1 in yeast results in a significant increase in atypical histone-DNA complexes and deregulated transcription activation and repression in vivo. In vitro thermodynamic nucleosome assembly assays (FRET, sedimentation), in vivo micrococcal nuclease assays in Δnap1 yeast, transcription reporter assays Molecular cell High 20347425
2011 Nap1 and the related chaperone Vps75 (both NAP1-family members, orthologs of NAP1L1) bind histones H3 and H4 in the tetrameric conformation as observed in the nucleosome. H3/H4 trapped in tetrameric state by these chaperones can be used as substrates for nucleosome assembly and chaperone-mediated lysine acetylation. Pulsed electron double resonance (PELDOR) measurements, protein crosslinking, in vitro nucleosome assembly, acetylation assays Molecular cell High 21329878
2012 NAP1-assisted nucleosome assembly is a two-step process as measured at the single-molecule level: NAP1 and core histones first compact DNA, and nucleosomes are assembled with a characteristic change in linking number (~56 nm compaction per nucleosome). Non-nucleosomal H3/H4 binding does not produce the linking number change that complete nucleosome assembly generates. Single-molecule magnetic tweezers measuring DNA end-to-end length and linking number changes in real time PloS one High 23050009
2013 Nap1 (NAP1L1 ortholog) shields the histone H2A-H2B interaction surfaces used within the nucleosome, protecting them from promiscuous DNA interactions. Hydrogen-deuterium exchange MS reveals H2A-H2B α-helices sample partially disordered conformations at low ionic strength; Nap1 binding reduces this conformational sampling. Two copies of H2A-H2B bound to a Nap1 homodimer form a tetramer through H2B–H2B contacts resembling a four-helix bundle. The Nap1–H2A-H2B interaction surface is confirmed as functionally relevant both in vitro and in vivo. Hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), mutagenesis, in vitro and in vivo functional validation Molecular cell High 23973327
2013 Drosophila NAP1 (ortholog of NAP1L1) is required for cohesin release and sister chromatid resolution during mitosis. NAP1 associates with the full cohesin complex and also forms a separate complex with the cohesin subunit SA/stromalin. NAP1 binding to cohesin is cell-cycle regulated, increasing in G2/M; this causes dissociation of PP2A from cohesin, increased SA phosphorylation, and cohesin removal. The balanced antagonism between NAP1 and PP2A controls mitotic cohesin dissociation. Proteomics, co-IP, genome-wide ChIP-seq (NAP1 and cohesin co-localization), genetic rescue experiments in Drosophila PLoS genetics High 24086141
2013 Yeast Nap1 (NAP1L1 ortholog) and Vps75 regulate histone H3-K9 acetylation during transcription elongation by modulating Rtt109 acetyltransferase activity. Loss of NAP1 suppresses cryptic transcription within ORFs seen in ctk1 deletion strains and reduces H3-K9 acetylation at the STE11 ORF, indicating Nap1 regulates Rtt109-dependent chromatin acetylation during elongation. Genetic suppression analysis, ChIP for histone modifications, genetic interactions in S. cerevisiae Molecular and cellular biology Medium 23401858
2014 NAP1L1 silencing (siRNA/shRNA) in pancreatic neuroendocrine neoplasm cells decreases proliferation by inhibiting mTOR pathway proteins and their phosphorylation. NAP1L1 binds directly to the p57(Kip2)/CDKN1C promoter (by ChIP, region -164 to +21) and promotes its methylation, thereby silencing p57(Kip2) expression. NAP1L1 knockdown reduces p57(Kip2) promoter methylation and upregulates p57(Kip2) transcript and protein, establishing NAP1L1 as an epigenetic regulator of the CDKN1C tumor suppressor. siRNA/shRNA knockdown, chromatin immunoprecipitation (ChIP) of NAP1L1 at CDKN1C promoter, bisulfite methylation analysis, mTOR pathway Western blotting, orthotopic mouse tumor model Epigenetics & chromatin High 25071868
2014 Nap1 (NAP1L1 ortholog) accumulates at DNA double-strand break (DSB) sites in human cells and DSB repair is substantially decreased in Nap1-knockdown cells. Nap1 binds RAD54, enhances RAD54-mediated nucleosome remodeling by evicting linker histone H1, and stimulates RAD51-mediated homologous pairing in higher-ordered chromatin containing histone H1. ChIP at DSB sites, siRNA knockdown DSB repair assay, in vitro RAD51/RAD54 homologous pairing assay with reconstituted chromatin, H1 eviction assay Scientific reports High 24798879
2015 Xenopus Nap1 (ortholog of NAP1L1) associates with the embryonic linker histone H1M in egg extracts; immunodepletion of Nap1 decreases H1M binding to mitotic chromosomes by ~50%, reduces H1M dynamics (FRAP), and causes chromosome decondensation similar to H1M depletion. Glutamylation of Nap1 (posttranslational modification) is required for proper H1M deposition; a glutamylation-deficient Nap1 mutant fails to rescue H1M dynamics or chromosome condensation, demonstrating that charge-shifting glutamylation of Nap1 controls linker histone dynamics essential for chromosome architecture. Xenopus egg extract immunodepletion, FRAP, chromosome condensation assays, add-back of wild-type vs. glutamylation-mutant Nap1 The Journal of cell biology High 25897082
2016 Yeast Nap1 (NAP1L1 ortholog) is a major regulator of H2A-H2B dynamics at the GAL locus: in NAP1-deleted cells, H2A-H2B accumulates at the repressed GAL locus on linker DNA independent of DNA sequence preference, and upon transcriptional activation H2A-H2B levels are further depleted in a NAP1-dependent manner. Nap1 is specifically required for transcription-dependent H2A-H2B exchange. ChIP for H2A-H2B and H3-H4 in Δnap1 vs. WT cells, in vivo histone exchange assay at GAL locus, in vitro nucleosome reconstitutions Molecular and cellular biology High 26884462
2017 NAP1L1 directly interacts with the ATP-dependent chromatin remodeler CSB (Cockayne syndrome protein B) and enhances CSB-mediated nucleosome remodeling. At the single-molecule level, NAP1L1 suppresses non-productive DNA-binding by CSB, accelerates both the activation and translocation phases of remodeling, and decreases the probability of CSB pausing during translocation, thereby increasing CSB processivity. This defines NAP1L1 as a regulatory cofactor that stimulates transcription-coupled nucleotide excision repair (TC-NER) by enhancing CSB remodeling activity. Single-molecule FRET (smFRET) and total internal reflection fluorescence microscopy to monitor CSB–DNA interactions and nucleosome remodeling in real time; in vitro reconstitution with purified NAP1L1 and CSB Nucleic acids research High 28369616
2017 HCV NS5A protein interacts with NAP1L1 and sequesters it in the cytoplasm, blocking NAP1L1 nuclear translocation. NS5A from genotype 2 (but not genotype 1) additionally targets NAP1L1 for proteasome-mediated degradation. Loss of NAP1L1 leads to decreased RELA protein levels and strongly impairs IRF3 phosphorylation by TBK1/IKKε, resulting in defective RIG-I and TLR3 antiviral signaling responses. Co-IP of NS5A and NAP1L1, domain mapping, subcellular fractionation, siRNA knockdown of NAP1L1, Western blotting for RELA and p-IRF3, RIG-I/TLR3 reporter assays in human hepatoma cells Journal of virology High 28659470
2018 NAP1L1 promotes proliferation of renal cancer cells partly through a KRAS-NAP1L1/P-ERK/ETS1 positive feedback axis; miR-532-5p directly targets both KRAS and NAP1L1 to suppress this pathway. ETS1 suppresses miR-532-5p transcription by binding its promoter, creating a feedback loop. Overexpression of NAP1L1 rescues the anti-proliferative effect of miR-532-5p. Luciferase reporter assay (3'UTR targeting), chromatin immunoprecipitation (ETS1 at miR-532-5p promoter), Western blotting for P-ERK, overexpression rescue experiments in RCC cells British journal of cancer Medium 30082686
2018 NAP1L1 is required for neural progenitor cell (NPC) proliferation and restraint of premature neuronal differentiation during cortical development. Nap1l1 knockdown and CRISPR-Cas9 knockout in mice decreases NPC proliferation and induces premature neuronal differentiation. RNA-seq identifies RassF10 as a downstream target; Nap1l1 promotes SETD1A-mediated H3K4 trimethylation at the RassF10 promoter to maintain RassF10 expression, and RassF10 overexpression rescues Nap1l1 KO neurogenesis defects. In utero electroporation knockdown, CRISPR-Cas9 knockout mice, RNA-seq, ChIP for H3K4me3 at RassF10 promoter, RassF10 rescue experiments Cell reports High 29490266
2018 PRDM8 (a PR domain protein) suppresses NAP1L1 expression in hepatocellular carcinoma cells; NAP1L1 activates the PI3K/AKT/mTOR signaling cascade, and PRDM8-mediated inhibition of HCC growth and metastasis is mediated through downregulation of NAP1L1. Lentiviral overexpression/knockdown of PRDM8, Western blotting for PI3K/AKT/mTOR phospho-proteins, rescue by NAP1L1 re-expression, in vivo tumor model Hepatology Medium 29572888
2018 lncRNA CDKN2B-AS1 promotes NAP1L1 expression by sponging miR-let-7c-5p; elevated NAP1L1 activates PI3K/AKT/mTOR signaling in HCC cells. NAP1L1 restoration abolishes the anti-proliferative and anti-metastatic effects of CDKN2B-AS1 knockdown, placing NAP1L1 downstream of the CDKN2B-AS1/let-7c-5p axis as a positive regulator of PI3K/AKT/mTOR. siRNA knockdown, luciferase reporter for miRNA sponging, Western blotting for p-AKT/p-mTOR, NAP1L1 rescue overexpression in HCC cells Cancer letters Medium 30165194
2019 Yeast Nap1 (NAP1L1 ortholog) serves as a dedicated ribosomal protein chaperone for Rps6 (small ribosomal subunit protein 6); Nap1 promotes solubility of Rps6 in vitro and interacts with a large, mostly eukaryote-specific binding surface of Rps6. Deletion of NAP1 enhances 40S synthesis defects of Rps6 mutants, demonstrating a co-evolutionary role of Nap1 in ribosome biogenesis beyond histone chaperoning. Tandem-affinity purification screen, in vitro solubility assay for r-proteins, genetic interaction analysis in S. cerevisiae Nucleic acids research Medium 31062022
2019 NAP1 (histone chaperone, NAP1L1 ortholog) mediates gene-specific eviction of linker histone H1 through a transcriptional activator→p300→NAP1→H1 pathway. In H1-compacted chromatin reconstituted in vitro, NAP1 is recruited by activator-bound p300 through direct interaction; NAP1 then facilitates core histone acetylation by p300 and concomitantly evicts H1 and H2A-H2B to enable transcription. In B cells, NAP1-mediated H1 eviction is required for induction of the CD40 gene. In vitro chromatin transcription reconstitution, co-IP of NAP1 with p300 and activators, H1 eviction assay, B cell CD40 gene induction assays with NAP1 depletion Molecular cell High 30902546
2021 NAP1L1 interacts with hepatoma-derived growth factor (HDGF) at the protein level; they co-localize in the cytoplasm. HDGF in turn interacts with the transcription factor c-Jun, which induces expression of cell cycle promoters CCND1/CDK4/CDK6. Knockdown of NAP1L1 in glioma cells inhibits proliferation and sensitizes cells to cisplatin, and this effect is reversed by HDGF overexpression, placing NAP1L1 upstream of the HDGF/c-Jun/CCND1 axis. Co-immunoprecipitation of NAP1L1 and HDGF, immunofluorescence co-localization, siRNA knockdown, Western blotting for CCND1/CDK4/CDK6, HDGF rescue overexpression, in vivo tumor model Aging Medium 34959221
2022 NAP1L1 interacts with HDGF in ovarian cancer cells (co-IP and immunofluorescence); HDGF recruits c-Jun to induce CCND1 expression, promoting G1/S progression. NAP1L1 knockdown blocks G1/S transition and induces apoptosis, and HDGF overexpression in NAP1L1-knockdown cells restores proliferation, confirming the NAP1L1→HDGF→c-Jun→CCND1 proliferative axis. Co-immunoprecipitation, immunofluorescence, siRNA/shRNA knockdown, flow cytometry cell cycle analysis, HDGF rescue in SKOV3/OVCAR3 cells BMC cancer Medium 35351053

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
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