| 2018 |
HSP90AB1 directly interacts with LRP5 (a Wnt co-receptor) via co-immunoprecipitation and GST pull-down, inhibiting ubiquitin-mediated proteasomal degradation of LRP5 and thereby stabilizing it; this stabilization activates AKT and Wnt/β-catenin signaling to promote epithelial-mesenchymal transition in gastric cancer cells. |
Co-immunoprecipitation, GST pull-down, in vitro ubiquitination assay, immunofluorescence, gain/loss-of-function in cell lines and xenograft mouse models |
Oncogene |
High |
30305727
|
| 2008 |
HSP90AB1 (HSP90beta) is a direct binding target of gamendazole; the drug binds purified yeast HSP82 (mammalian HSP90AB1 homologue), inhibits its luciferase-refolding (chaperone) activity, causes degradation of HSP90-dependent client proteins AKT1 and ERBB2, and does not compete with geldanamycin or novobiocin for binding, suggesting a distinct binding site. |
Biotinylated affinity purification, MALDI-TOF mass spectrometry, Western blot, in vitro luciferase refolding assay with purified HSP82 |
Biology of reproduction |
High |
18218611
|
| 2021 |
EEF1A2 physically interacts with HSP90AB1 (confirmed by LC-MS/MS and Co-IP), and this interaction increases TGFβ receptor I and II expression, followed by enhanced SMAD3 phosphorylation and nuclear localization, promoting EMT in lung adenocarcinoma cells. |
LC-MS/MS interactome, co-immunoprecipitation, immunofluorescence, in vitro and in vivo functional assays |
British journal of cancer |
Medium |
33473168
|
| 2022 |
HSP90AB1 physically interacts with B7-1 in podocytes via residue K69 in the N-terminal domain of HSP90AB1 (identified by LC-MS/MS and confirmed by molecular docking and mutant analysis), acting as a scaffold to transmit signals from B7-1 to LRP5/β-catenin, thereby mediating podocyte injury and glomerulosclerosis. |
LC-MS/MS, molecular docking, site-directed mutagenesis, co-immunoprecipitation, transgenic/adriamycin nephropathy mouse models |
Cell death and differentiation |
High |
35710882
|
| 2021 |
HSP90AB1 interacts with the coiled-coil (CC) domain of Bcr-Abl via its N-terminal domain (NTD), retaining Bcr-Abl in the cytoplasm and maintaining Bcr-Abl tyrosine kinase activation; disruption of this interaction (by 17AAG targeting NTD) permits nuclear translocation of Bcr-Abl, which activates p73 and induces apoptosis of CML cells. |
Immunoprecipitation-mass spectrometry, immunoprecipitation with domain mapping, immunofluorescence, Western blot, CCK-8, flow cytometry |
Cell communication and signaling |
Medium |
34217296
|
| 2022 |
HSP90AB1 immunoprecipitates latent TGFβ (from osteoblast-secreted proteomes) and inactivates it; extracellular HSP90AB1 also inhibits tumor cell growth and osteoclast maturation in a mouse model of osteolysis. |
Immunoprecipitation (from conditioned medium proteomes), whole-genome proteomics, gain/loss-of-function, in vivo mouse osteolysis model |
Theranostics |
Medium |
34976221
|
| 2019 |
USP22 deubiquitylase positively regulates HSP90AB1 expression at the transcriptional level via maintenance of H3K9 acetylation on the HSP90AB1 gene; siRNA knockdown of USP22 reduces H3K9ac at the HSP90AB1 locus and decreases HSP90AB1 mRNA and protein in colorectal and breast cancer cells and in tissue-specific Usp22 knockout mice. |
siRNA knockdown, mRNA-seq, Western blot, ChIP (H3K9ac), mouse tissue-specific Usp22 knockout |
Cell death & disease |
Medium |
31801945
|
| 2022 |
RGNNV capsid protein (CP) binds the NM domain of fish HSP90ab1 (LjHSP90ab1) on the cell surface, competitively blocking AKT interaction with HSP90ab1, thereby inhibiting the AKT-mTOR pathway and inducing incomplete autophagy (impaired autophagosome-lysosome fusion) during early viral infection. |
Co-immunoprecipitation, domain mapping, Western blot, autophagy flux assays in fish cell lines |
Zoological research |
Medium |
34904422
|
| 2023 |
HSP90AB1 interacts with the N, NS7, and NSP10 proteins of PDCoV (porcine deltacoronavirus); the C-tail domain of the N protein mediates interaction with HSP90AB1, and HSP90AB1 protects N protein from proteasomal degradation. ATPase activity of HSP90AB1 is required for PDCoV infection (ATPase-inhibiting HSP90 inhibitors suppressed infection, but KW-2478, which does not affect ATPase, had no effect). |
Genome-wide CRISPR screen, Co-IP, domain deletion mapping, HSP90 inhibitor treatment, proteasome inhibitor rescue assay, viral titer measurement |
Journal of biological chemistry |
High |
38092149
|
| 2024 |
SENP1-mediated deSUMOylation of HSP90ab1 at Lys72 suppresses STAT3 activation and fibronectin secretion in cardiomyocytes; loss of SENP1 increases HSP90ab1 SUMOylation, activates STAT3, and drives paracrine fibroblast activation and cardiac fibrosis after myocardial infarction. Mutation of HSP90ab1 Lys72 (SUMOylation site) ameliorates adverse ventricular remodeling. |
Cardiomyocyte-specific SENP1 KO and overexpression mice, site-directed mutagenesis (K72 mutation), Western blot, cardiac function measurement, histology |
Advanced science |
High |
38992961
|
| 2023 |
DSCC1 interacts with HSP90AB1 (confirmed by co-immunoprecipitation) and promotes ER stress-mediated progression of lung adenocarcinoma; knockdown of either protein reduces LUAD cell proliferation, stemness, EMT, and metastatic potential. |
Co-immunoprecipitation, siRNA knockdown, in vitro cell assays, in vivo tumor models |
Cancer cell international |
Low |
37742009
|
| 2016 |
HSP90AB1 knockdown reduces phospho-AKT (Ser473) levels in head and neck squamous cell carcinoma cells, placing HSP90AB1 upstream of AKT activation in HNSCC. |
Lentiviral shRNA knockdown, Western blot for phospho-AKT, CCK-8/EdU/colony/transwell/xenograft assays |
Technology in cancer research & treatment |
Low |
35929142
|
| 2022 |
HSP90AB1 knockdown in T cells reduces p-AKT, SMARCC1, p-c-Fos, and p-c-Jun expression and increases ROS and apoptosis; overexpression of HSP90AB1 inhibits capecitabine-induced T cell apoptosis by sustaining the AKT/SMARCC1/AP-1 axis and reducing ROS, establishing HSP90AB1 as a pro-survival regulator in T cells via this signaling cascade. |
siRNA knockdown, overexpression, quantitative proteomics/phosphoproteomics, Western blot, ROS measurement, flow cytometry apoptosis assay |
Oxidative medicine and cellular longevity |
Medium |
35368874
|
| 2023 |
PARP1 interacts with HSP90AB1 (confirmed by Co-IP), and HSP90AB1 counteracts PARP1's repression of BLM promoter activity; HSP90AB1 thus acts as a co-regulator that de-represses BLM transcription in prostate cancer cells. |
Co-immunoprecipitation, DNA pull-down with promoter probe, dual luciferase reporter assay, ChIP-qPCR, MS |
Journal of translational medicine |
Medium |
37415147
|
| 2023 |
CDK1-SRC interaction transcriptionally activates HSP90AB1 expression in hepatocellular carcinoma; manipulation of SRC or HSP90AB1 reverses the effects of CDK1 and SRC on HCC cell proliferation and migration, placing HSP90AB1 downstream of the CDK1-SRC kinase network. |
In vitro and in vivo functional assays, transcriptomic/proteomic analysis, siRNA/overexpression experiments |
Journal of proteome research |
Low |
37949475
|
| 2018 |
Calenduloside E (CE) directly binds purified recombinant HSP90AB1 protein, as confirmed by competitive binding assay with CE-P probe and surface plasmon resonance (SPR) kinetic analysis showing dose-dependent binding. |
Clickable activity-based probe affinity purification, proteomic identification, competitive binding assay with purified recombinant HSP90AB1, SPR |
Frontiers in pharmacology |
Medium |
29875664
|
| 2023 |
HSP90AB1 is required for transmissible gastroenteritis virus (TGEV) infection; knockdown of HSP90AB1 (but not HSP90AA1) and treatment with VER-82576 (an ATPase-inhibiting HSP90 inhibitor) reduce TGEV mRNA, N protein, and virus titers in a dose-dependent manner, with the inhibitory effect occurring mainly at early viral replication. |
siRNA knockdown, KO cells, HSP90 inhibitor time-of-addition assay, viral titer measurement, RT-qPCR, Western blot |
International journal of molecular sciences |
Medium |
37958953
|
| 2025 |
LGR5 directly binds HSP90AB1 (confirmed by GST pull-down and Co-IP), and this interaction promotes phosphorylation of GSK-3β, leading to β-catenin stabilization and nuclear translocation that activates AR transcription, conferring enzalutamide resistance in prostate cancer; reducing HSP90AB1-LGR5 binding restores enzalutamide sensitivity. |
GST pull-down, co-immunoprecipitation, immunofluorescence, Western blot, in vitro and in vivo functional assays |
Chinese medical journal |
Medium |
40280884
|
| 2025 |
Polydatin specifically binds HSP90AB1 at the Asp88 residue and disrupts HSP90AB1-mediated stabilization of the client protein ACT1, thereby suppressing the IL-17/MAPK/NF-κB inflammatory pathway in acute lung injury models. |
CETSA, thermal proteome profiling, mass spectrometry, site-directed mutagenesis, molecular docking, MST, cell lines overexpressing HSP90AB1, Western blot, in vivo rat ALI model |
Journal of ethnopharmacology |
High |
41707809
|
| 2025 |
Bruceine A (BRA) binds HSP90AB1 at the Ser-108 residue and inhibits its chaperone function; downstream HSP90AB1 client/partner proteins PIK3CG, EGFR, and KDM5C are destabilized, suppressing HCC cell proliferation and inducing apoptosis. |
Chemical proteomics (MST, SPR, CETSA), site-directed mutagenesis, HSP90AB1 knockdown, TMT-based proteomics for downstream clients, patient-derived organoids and xenograft models |
Journal of advanced research |
High |
40664262
|
| 2026 |
ACOX1-dependent increase in crotonyl-CoA under hypoxia drives site-specific crotonylation of HSP90AB1 at Lys265; molecular dynamics simulations show K265 crotonylation induces conformational compaction of HSP90AB1, strengthening its interaction with client protein TXN (thioredoxin) and enhancing TXN stability to buffer ROS and confer cisplatin resistance in oral squamous cell carcinoma. |
Molecular dynamics simulation, site-directed mutagenesis (K265R), co-immunoprecipitation, Western blot, in vitro and in vivo tumor models, pharmacological inhibition of ACOX1 |
Research (Washington, D.C.) |
Medium |
41675575
|
| 2025 |
Chemerin stimulates SUMO2/3 conjugation to HSP90AB1 in monocytes via β2 integrin signaling; this SUMOylation of HSP90AB1 is essential for downstream ERK1/2 phosphorylation and monocyte activation and adhesion, as shown by immunoprecipitation/LC-MS/MS identification and reversal with SUMOylation inhibitor ML-792. |
Immunoprecipitation, LC-MS/MS, SUMOylation inhibitor (ML-792), Western blot, monocyte adhesion assay |
Cellular signalling |
Medium |
40744335
|
| 2026 |
HSP90AB1 interacts with ITGBL1 and mediates its K63-linked ubiquitination and degradation; loss of this HSP90AB1-dependent degradation of ITGBL1 activates ER stress-induced autophagy, suppressing osteosarcoma progression. |
Co-IP, domain mapping, ubiquitination assay (K63-linkage), in vitro and in vivo functional assays, virtual screening and Co-IP for inhibitor (ivermectin) |
Advanced science |
Medium |
41697125
|
| 2025 |
IGF2BP3 (m6A reader) binds m6A-tagged HSP90AB1 mRNA and stabilizes it in an m6A-dependent manner, increasing HSP90AB1 protein levels which activate the PI3K/AKT signaling pathway to promote bladder cancer progression. |
RNA-seq, m6A-seq, RIP-seq, RIP-qPCR, site-directed mutagenesis of m6A sites, Western blot, in vitro and in vivo assays |
FEBS journal |
Medium |
40105114
|
| 2025 |
HNRNPH1 binds HSP90AB1 mRNA and inhibits its protein expression; this suppresses HSP90AB1-mediated inhibition of MAP1LC3B-dependent autophagy, thereby restraining lung adenocarcinoma malignant phenotype. |
RIP (RNA binding protein immunoprecipitation), siRNA/overexpression, Western blot, in vivo tumor models, autophagy flux assays |
Respiratory research |
Low |
40468317
|
| 2024 |
GLCCI1 directly interacts with HSP90AB1 (confirmed by Co-IP), and HSP90AB1 in turn interacts with GRP78; GLCCI1 acts as an upstream regulator of HSP90AB1, which then regulates GRP78-initiated ER stress-induced apoptosis in retinal ganglion cells during diabetic retinopathy. |
Co-immunoprecipitation, GLCCI1 overexpression/knockdown, Western blot for GRP78/CHOP/caspase-3, in vivo DR mouse model |
Scientific reports |
Medium |
39496608
|
| 2022 |
HSP90ab1 and Myh9 (non-muscle myosin) interact via immunoprecipitation; extracellular HSP90ab1 and Myh9 secreted by PI3K-activated MSCs exert anti-tumor effects and inhibit osteoclast maturation. |
Immunoprecipitation from conditioned medium, mass spectrometry, in vitro and in vivo tumor suppression assays |
Molecular therapy oncolytics |
Low |
36090473
|
| 2025 |
SP1 transcription factor drives HSP90ab1 transcription by binding its promoter; pharmacological inhibition of SP1 reduces Hsp90ab1 expression; Hsp90ab1 in turn stabilizes the client protein COX-2 via p38/JNK signaling in uterine tissue, mediating primary dysmenorrhea. |
Promoter binding analysis (SP1 ChIP implied), geldanamycin inhibition of Hsp90ab1, lentiviral Hsp90ab1 overexpression reversal, Western blot, in vivo mouse PD model |
Bioorganic chemistry |
Medium |
39914036
|
| 2020 |
HSP90ab1 specifically adsorbs to denatured (misfolded) proteins in nanoparticle protein coronas; the level of HSP90ab1 adsorption correlates with circular dichroism and ANS fluorescence measures of protein denaturation, validating that HSP90ab1 functions as a chaperone that selectively binds misfolded/denatured client proteins in vitro. |
Western blot of NP-corona complex, circular dichroism, ANS fluorescence spectroscopy, comparison across NP types and surface modifications |
Nanoscale |
Low |
32696774
|
| 2025 |
NB (Dictamni Cortex nanoparticles) suppresses HSP90AB1 transcription by inhibiting its activator CTCF, and disrupts the HSP90AB1-CDC37 co-chaperone complex, thereby inactivating client proteins STAT3 and AKT in keratinocytes. |
Nascent proteomics, Western blot, co-chaperone complex disruption assay, in vitro keratinocyte and in vivo mouse psoriasis model |
Advanced science |
Low |
41114929
|