| 2004 |
HN1 (JPT1) encodes a 16.5-kDa protein that localizes to the nucleus, as determined by GFP fusion expression and Western blot in transfected cells. |
GFP fusion expression, Western blot, subcellular localization imaging |
Gene |
Medium |
15094197
|
| 2009 |
Hn1 depletion in B16.F10 melanoma cells promotes differentiation, including increased melanogenesis (elevated tyrosinase and Trp2), increased actin–Rab27a interaction, G1/S cell cycle arrest (reduced pRb phosphorylation, lower p27, increased p21), reduced c-Met expression, reduced basal ERK phosphorylation, increased basal p38 MAPK phosphorylation, and reduced transcription factors MITF and USF-1 with increased TFE3. |
siRNA knockdown, flow cytometry, Western blot, immunofluorescence in murine melanoma cells |
Differentiation; research in biological diversity |
Medium |
19427096
|
| 2011 |
HN1 is regulated by androgens via androgen response elements in its promoter. HN1 overexpression promotes ubiquitination-mediated proteasomal degradation of androgen receptor (AR) by reducing AR S213/210 phosphorylation, thereby downregulating AR target genes (KLK3, KLK4, NKX3.1, STAMP2). HN1 knockdown increases Akt(S473) phosphorylation and promotes AR nuclear translocation, an effect blocked by the Akt inhibitor LY294002 but not ERK inhibitor PD98059. |
siRNA knockdown, overexpression, Western blot, qRT-PCR, co-treatment with kinase inhibitors in prostate cancer cell lines |
Molecular and cellular endocrinology |
Medium |
22155408
|
| 2015 |
HN1 physically associates with the GSK3β/β-catenin destruction complex and is predominantly cytoplasmic when GSK3β is phosphorylated at S9. Ectopic HN1 expression increases β-catenin degradation, leading to loss of E-cadherin interaction, actin reorganization, colony formation and migration in PC-3 and MDA-MB231 cancer cells. |
Co-immunoprecipitation, Western blot, overexpression, immunofluorescence, migration/colony assays |
Journal of cellular biochemistry |
Medium |
25169422
|
| 2017 |
HN1 promotes breast cancer cell migration, invasion, tumorigenesis and cancer stem cell expansion by upregulating MYC expression and its target genes (CDK4, CCND1, p21, CAV1, SFRP1). MYC knockdown abrogates the effects of HN1 overexpression. |
Overexpression, siRNA knockdown, qRT-PCR, Western blot, mammosphere assay, transwell assay, xenograft model, epistasis rescue |
Molecular cancer |
Medium |
28490334
|
| 2019 |
HNRNPA1 regulates the 3′ UTR length of HN1 (JPT1) through alternative polyadenylation (APA): downregulation of HNRNPA1 induces 3′ UTR lengthening of HN1, producing less stable transcripts and less protein, and induces senescence-associated phenotypes that are partially reversed by HN1 overexpression. |
APA analysis, siRNA knockdown of HNRNPA1, HN1 overexpression rescue, senescence assays, Western blot |
Aging |
Medium |
31257225
|
| 2020 |
HN1 interacts with STMN1 (Stathmin 1), prevents STMN1 ubiquitination and proteasomal degradation, and increases STMN1 mRNA expression. HN1 reduces α-tubulin acetylation and promotes EMT in anaplastic thyroid carcinoma (ATC). Loss of STMN1 reduces the malignant potential conferred by HN1; HN1 knockdown combined with STMN1 overexpression restores aggressive ATC cell properties. |
Co-immunoprecipitation, Western blot, qRT-PCR, overexpression/knockdown, xenograft model, epistasis |
Cancer letters |
Medium |
33359451
|
| 2021 |
HN1 co-localizes with γ-tubulin foci at centrosomes in prostate cancer cells and physically interacts with γ-tubulin by immunoprecipitation. HN1 depletion increases γ-tubulin foci and disrupts microtubule spindle assembly, implicating HN1 in centrosome clustering. |
Immunofluorescence co-localization, co-immunoprecipitation, siRNA knockdown, immunoprecipitation in PC-3 cells |
Cell cycle (Georgetown, Tex.) |
Medium |
34382911
|
| 2022 |
HN1 sustains MYC stability and activity in hepatocellular carcinoma by interacting with GSK3β and preventing GSK3β-mediated phosphorylation and ubiquitin-proteasomal degradation of MYC. Co-immunoprecipitation confirmed HN1–MYC protein interaction. MYC suppression attenuates HN1-driven HCC proliferation and metastasis. |
Co-immunoprecipitation, Western blot, luciferase reporter for MYC transcriptional activity, qRT-PCR, in vitro and xenograft models |
Cell biology international |
Medium |
36403281
|
| 2022 |
HN1 prevents HMGB1 protein from ubiquitination and autophagy-lysosome pathway degradation through interaction with TRIM28. In the nucleus, reduced HMGB1 following HN1 knockdown increases DNA damage and cell death in oxaliplatin-treated HCC cells; in the cytoplasm, HN1 regulates autophagy via HMGB1. HMGB1 overexpression rescues the phenotypes induced by HN1 knockdown. |
Co-immunoprecipitation, Western blot, ubiquitination assay, autophagy assays, gain/loss-of-function, rescue experiments, xenograft model |
The FEBS journal |
Medium |
35596723
|
| 2023 |
HN1 overexpression in prostate cancer cells (post-G2) leads to S-phase accumulation and early mitotic exit. Mechanistically, HN1 interacts with Cyclin B1 and Cdh1 (APC/C co-factor) by co-immunoprecipitation, and promotes Cyclin B1 ubiquitination and degradation by stabilizing Cdh1. Stably HN1-expressing cells show reduced Cdt1 loading onto chromatin, consistent with G1-to-S transition. |
Co-immunoprecipitation, Western blot, flow cytometry, immunofluorescence, cellular fractionation, inducible overexpression, ubiquitination assay |
Biology |
Medium |
36829467
|
| 2023 |
HN1 promotes dedifferentiation of anaplastic thyroid cancer cells by inhibiting CTCF expression via epigenetic silencing: HN1 recruits HDAC2 to the CTCF promoter, reducing H3K27 acetylation and suppressing CTCF transcription. ATAC-seq and ChIP-seq showed CTCF regulates chromatin accessibility at thyroid differentiation genes. CTCF overexpression reverses HN1-driven dedifferentiation phenotypes. |
ATAC-seq, ChIP-seq, Co-immunoprecipitation (HN1–HDAC2), Western blot, qRT-PCR, overexpression/knockdown epistasis, xenograft and zebrafish models |
Cancer letters |
High |
37993084
|
| 2022 |
HN1 knockdown in prostate cancer cells sensitizes them to docetaxel- and 2-methoxyestradiol-induced apoptosis (measured by PARP cleavage and Caspase-3 activity). Conversely, HN1 overexpression inhibits drug-induced apoptosis. Simultaneous knockdown of Cyclin B1 and HN1 abolishes the increased apoptotic response caused by HN1 knockdown alone, placing HN1's anti-apoptotic function upstream of Cyclin B1. |
siRNA knockdown, cDNA overexpression, PARP cleavage Western blot, Caspase-3 activity assay, epistasis (Cyclin B1 co-KD) |
Annals of clinical and laboratory science |
Medium |
35414498
|
| 2024 |
HN1 co-localizes with Aurora A and Eg5 at centrioles and maintains their co-localization with PLK1 and PCM1. HN1 depletion (siRNA/shRNA) disrupts Aurora A and PLK1 co-localizations with Eg5 and PCM1, reduces Aurora A and PLK1 phosphorylation, and increases dysregulated mitotic spindle structures, nuclear and cytokinetic abnormalities, and supernumerary but immature centrosomes. HN1 overexpression suppresses aberrant spindle formation and ensures fidelity of centriole/centrosome duplication. |
Immunofluorescence co-localization, siRNA/shRNA knockdown, overexpression, Western blot for Aurora A and PLK1 phosphorylation |
Cytoskeleton (Hoboken, N.J.) |
Medium |
39291428
|
| 2024 |
HN1 activates the Akt–SREBP signaling axis to promote lipogenesis in HCC: HN1 overexpression increases SREBP1 and SREBP2 expression and lipid formation, while HN1 silencing decreases them. HN1 silencing downregulates 379 genes enriched in the lipogenic signaling pathway and suppresses HCC xenograft growth. |
Gene expression profiling, Western blot, lipid staining, overexpression/knockdown, xenograft model |
Cancer gene therapy |
Medium |
39251779
|
| 2024 |
HN1 expression is cell-cycle-phase-dependent in neuroblastoma SH-SY5Y cells, peaking in S-phase and lower in other phases. HN1 overexpression increases the ratio of undifferentiated (S-type) cells and alters cell cycle dynamics, functioning as a dedifferentiation factor. HN1 expression correlates with microtubule stability (nocodazole/taxol treatment experiments). |
Flow cytometry (cell cycle phasing), bioinformatics co-expression analysis, nocodazole/taxol treatment, overexpression, in vitro differentiation model |
Journal of cellular biochemistry |
Low |
38629746
|
| 2025 |
HN1 is required for nucleolar organizer region (NOR) integrity and function, and is a component of the mTOR–RPS6 axis. HN1 depletion reduces mRNA translation in mammalian cancer cells, causes irregular distribution of nucleolar structures, and leads to aggregation of translation machinery components with loss of essential interactions. Immunoprecipitation confirmed HN1 association with components of the mTOR–RPS6 signaling pathway. |
Co-immunoprecipitation, immunofluorescence co-localization, Western blot, gain/loss-of-function, mRNA translation assays, nucleolar integrity assays |
Cell proliferation |
Medium |
39805577
|
| 2025 |
HN1 forms a complex with transcription factor CEBPB, preventing CEBPB ubiquitination and degradation, thereby promoting CCL2 transcription in anaplastic thyroid carcinoma cells. HN1-driven CCL2 secretion induces VSIG4+ tumor-associated macrophage differentiation via CCR2/PI3K/AKT pathway activation. |
Cytokine array screening, co-culture validation, co-immunoprecipitation (HN1–CEBPB), ubiquitination assay, CCL2-neutralizing antibody, knockdown experiments, in vivo xenograft model |
Biochimica et biophysica acta. Molecular basis of disease |
Medium |
42191099
|