| 1997 |
RUVBL1 (TIP49) was identified as a TBP-interacting protein that forms a complex with TBP in nuclear extracts, isolated by affinity purification using histidine-tagged TBP. The protein contains Walker A and B motifs and shows structural similarity to bacterial RuvB, suggesting ATP-dependent enzymatic activity. |
Affinity purification (histidine-tagged TBP), immunoprecipitation, sequence analysis |
Biochemical and biophysical research communications |
Medium |
9196036
|
| 1998 |
RUVBL1 (Pontin52) was identified as a nuclear protein that binds beta-catenin in the region of Armadillo repeats 2–5 and also binds TBP, forming an in vivo multiprotein complex with beta-catenin and LEF-1/TCF. This implicated RUVBL1 in the nuclear transcriptional function of beta-catenin. |
Yeast two-hybrid (identification), co-immunoprecipitation (in vivo complex validation), domain mapping |
Proceedings of the National Academy of Sciences of the United States of America |
High |
9843967
|
| 1998 |
RUVBL1 was identified as a human protein homologous to RuvB; it co-immunoprecipitated with cellular proteins and was detected in the RNA polymerase II holoenzyme complex. Null mutation of the yeast homolog scRUVBL1 was nonviable, demonstrating it is essential for cell survival. |
Yeast two-hybrid (identification via RPA3 bait), co-immunoprecipitation, multi-step chromatographic purification, yeast null mutation |
The Journal of biological chemistry |
High |
9774387
|
| 1999 |
RUVBL1 (TIP49a/TIP49) is an ATP-dependent DNA helicase with ssDNA-stimulated ATPase activity that unwinds DNA duplexes in the 3' to 5' direction, as established by in vitro enzyme assays with purified recombinant protein. |
In vitro ATPase assay, DNA helicase assay, UV cross-linking, recombinant protein purification |
The Journal of biological chemistry |
High |
10336418
|
| 1999 |
RUVBL1 (TIP49a) and RUVBL2 (TIP49b) bind each other and are found together in the same ~700 kDa complex in cells. TIP49b has opposite DNA helicase polarity (5' to 3') compared to TIP49a (3' to 5'), and TIP49b does not complement the TIP49a yeast null mutation, indicating non-redundant functions. |
Co-immunoprecipitation, gel filtration (complex size), in vitro ATPase and helicase assays, yeast complementation |
The Journal of biological chemistry |
High |
10428817
|
| 2000 |
RUVBL1 (Pontin52) and RUVBL2 (Reptin52) interact with each other and both bind beta-catenin and TBP, but act antagonistically on beta-catenin/TCF transactivation in reporter gene assays. This antagonism is conserved in Drosophila (dpontin vs. dreptin in Wingless signaling). |
Reporter gene assay (transactivation), co-immunoprecipitation, Drosophila in vivo genetics |
The EMBO journal |
High |
11080158
|
| 2001 |
RUVBL1 (TIP49a) functions as a plasminogen-binding protein on the U937 cell surface via a C-terminal lysine; it binds human plasminogen with a Kd of 0.57 μM and enhances plasminogen activation 8-fold, as demonstrated by ligand blotting and plasminogen activation assays. |
2D gel electrophoresis, ligand blotting with 125I-plasminogen, carboxypeptidase B sensitivity assay, kinetic binding assay, plasminogen activation assay |
The Journal of biological chemistry |
Medium |
11027681
|
| 2002 |
RUVBL1 (TIP49) modulates c-Myc-mediated apoptosis and also binds the E2F1 transactivation domain to modulate E2F1-dependent transforming and apoptotic activities, while the related factor TRRAP does not affect apoptosis. This distinguishes RUVBL1 as a specific cofactor for these transcription factors. |
Co-immunoprecipitation (E2F1 binding), functional apoptosis assays, dominant-negative mutant analysis |
Oncogene |
Medium |
12185582
|
| 2003 |
RUVBL1 (TIP49) ATPase activity is required for beta-catenin-mediated neoplastic transformation and activation of TCF-dependent genes. An ATPase-deficient mutant (TIP49D302N) inhibited these activities. RUVBL1 was found in complexes with TIP60, TRRAP, and BAF53 chromatin-remodeling factors at the ITF-2 promoter, and its inhibition reduced histone acetylation near TCF-binding sites. |
ATPase-deficient mutant (D302N) expression, reporter gene assay, siRNA knockdown, chromatin immunoprecipitation (ChIP), co-immunoprecipitation |
Cancer research |
High |
14695187
|
| 2003 |
RUVBL1 associates with alpha- and gamma-tubulin and localizes to the centrosome and mitotic spindle during mitosis, where its topology varies with mitotic stage. RUVBL1 promotes in vitro tubulin assembly. |
Protein affinity chromatography, co-immunoprecipitation, confocal immunofluorescence microscopy, GST pulldown, in vitro tubulin assembly assay |
Cell motility and the cytoskeleton |
Medium |
14506706
|
| 2006 |
The crystal structure of human RuvBL1 hexamer was solved at 2.2 Å resolution in complex with ADP. The structure revealed three domains: domains I and III mediate ATP binding/hydrolysis, while domain II (unique to eukaryotes, absent from bacterial RuvB) is a novel DNA/RNA-binding domain. RuvBL1 binds single-stranded DNA/RNA and double-stranded DNA, but shows only marginal ATPase activity in isolation, suggesting requirement for cofactors. |
X-ray crystallography (2.2 Å), DNA binding assays, ATPase activity assay |
The Journal of biological chemistry |
High |
17060327
|
| 2006 |
Human TIP48 and TIP49 form a stable equimolar dodecameric complex (two stacked hexameric rings) with synergistic ATPase activity. Both proteins are required for ATPase activity (catalytic mutants in either abolish activity). No DNA helicase or branch migration activity was detected in the reconstituted complex. |
In vitro reconstitution, ATPase assay, ATPase-deficient mutants, negative stain electron microscopy (3D reconstruction at 20 Å) |
Journal of molecular biology |
High |
17157868
|
| 2008 |
Human RUVBL1 (Rvb1) is required for the histone acetyltransferase (HAT) activity of the Tip60/NuA4 complex but not for Ino80 or SRCAP complexes. RUVBL1 depletion increases persistence of phospho-H2AX after DNA damage, and this phenotype is phenocopied by Tip60 depletion. Histone H4 acetylation by Tip60 is required prior to dephosphorylation of phospho-H2AX. |
siRNA knockdown, in vitro HAT activity assay, immunofluorescence, H4 acetylation assay, epistasis between Rvb1 and Tip60/Ino80/SRCAP |
Molecular and cellular biology |
High |
18285460
|
| 2008 |
Yeast Rvb1 and Rvb2 form a heterohexameric ring with enhanced ATPase activity compared to individual proteins; ATPase is further stimulated by dsDNA with 5' or 3' overhangs. The complex exhibits ATP-dependent DNA helicase activity preferring 5' to 3' unwinding. |
In vitro reconstitution, ATPase assay, electron microscopy, DNA helicase assay |
Journal of molecular biology |
High |
18234224
|
| 2008 |
RUVBL1 depletion reduced RAD51 recruitment to chromatin and nuclear foci formation after DSBs and interstrand crosslinks by ~50%, without affecting DNA damage checkpoint signaling (H2AX phosphorylation). Histone deacetylase inhibitor treatment restored RAD51 foci, linking RUVBL1 to chromatin modification-dependent homologous recombination repair. |
siRNA knockdown, RAD51 foci immunofluorescence, chromatin fractionation, HDAC inhibitor rescue experiment |
The international journal of biochemistry & cell biology |
Medium |
18834951
|
| 2009 |
TIP48 and TIP49 play a major role in catalyzing H2A acetylation-induced H2A.Z exchange into nucleosomes via their ATPase activities. TIP60-mediated acetylation of nucleosomal H2A specifically facilitates the action of the complex containing TIP48/TIP49 in the H2A.Z exchange reaction. |
Purification of H2A.Z-interacting complexes, in vitro H2A.Z exchange assay, TIP60 HAT assay, ATPase-dependent mechanistic dissection |
Nucleic acids research |
High |
19696079
|
| 2010 |
RUVBL1 and RUVBL2 associate with each PIKK family member (ATM, ATR, mTOR, DNA-PKcs, SMG-1, TRRAP), control PIKK mRNA and protein abundance upon knockdown, and promote the assembly of SMG-1-containing mRNA surveillance complexes in the cytoplasm during nonsense-mediated mRNA decay (NMD). |
Co-immunoprecipitation (RUVBL1/2 with PIKKs), siRNA knockdown (PIKK abundance and NMD), mRNP complex assembly assay |
Science signaling |
High |
20371770
|
| 2011 |
RUVBL1 represses p53 transcription by binding to the p53 promoter, interfering with RNF20/hBRE1-mediated histone H2B monoubiquitination, and promoting PAF1-mediated histone H3K9 trimethylation. This mechanism underlies RUVBL1's ability to block p53-mediated apoptosis downstream of EHF transcription factor activation. |
ChIP, co-immunoprecipitation, siRNA knockdown, reporter assay, histone modification analysis |
EMBO reports |
Medium |
21617703
|
| 2011 |
The RuvBL1-RuvBL2 heterodimeric complex forms a dodecamer of two heterohexameric rings with alternating RUVBL1/RUVBL2 subunits bound to ADP/ATP. Truncation of domain II substantially increases ATPase activity, and domain II auto-inhibits helicase activity—showing that in vivo activities are regulated by cofactors via domain II conformational changes. |
X-ray crystallography (dodecamer with truncated DII), SAXS, ATPase assay, helicase assay |
Journal of structural biology |
High |
21933716
|
| 2011 |
Hsp90 forms complexes with the RUVBL1/2 complex and the Tel2 complex, and Hsp90 inhibition reduces abundance of all PIKK family members and suppresses PIKK-mediated signaling, demonstrating that Hsp90 regulates PIKKs together with RUVBL1/2. |
Co-immunoprecipitation, Hsp90 inhibitor treatment, immunoblot for PIKK levels |
Cancer science |
Medium |
21951644
|
| 2012 |
Cryo-EM of the human RuvBL1-RuvBL2 complex revealed two coexisting conformations (compact and stretched) driven by movements in domain II (DII). DII domains connect the AAA+ core and expose DNA-binding regions, suggesting that these conformational transitions regulate the activity of RUVBL1-RUVBL2-containing complexes. |
Cryo-electron microscopy (~15 Å), image classification, nucleic acid binding analysis |
Nucleic acids research |
High |
23002137
|
| 2012 |
The TTT-RUVBL1/2 complex (TELO2-TTI1-TTI2 plus RUVBL1/2) is required for mTORC1 assembly into obligate dimers, its lysosomal localization, and its interaction with Rag GTPases. Energy depletion (loss of ATP from glucose/glutamine) disassembles and represses the TTT-RUVBL complex, thereby impairing mTORC1 function. |
Co-immunoprecipitation, siRNA knockdown, lysosome fractionation, AMPK/TSC epistasis analysis, metabolic flux assays |
Molecular cell |
High |
23142078
|
| 2013 |
RuvbL1 and RuvbL2 function as disaggregases: they directly interact with aggregated substrate synphilin-1 near the opening of the central channel of the barrel structure, polypeptides with unfolded structures and amyloid fibrils stimulate RuvbL ATPase activity, and the complex promotes disassembly of protein aggregates and aggresome formation. |
siRNA screen, Co-IP (synphilin-1 interaction), ATPase stimulation assay (amyloid fibrils), aggregate disaggregation assay, yeast genetic studies |
The EMBO journal |
High |
26303906
|
| 2014 |
RuvBL1 and RuvBL2 co-purify with the Fanconi anemia (FA) core complex under native conditions, and depletion of RuvBL1-RuvBL2 leads to co-depletion of the FA core complex, causes DNA crosslinker sensitivity, chromosomal instability, and defective FA pathway activation. Conditional Ruvbl1 knockout in mouse hematopoietic cells causes aplastic anemia. |
Affinity purification-MS, co-immunoprecipitation, siRNA depletion, mouse conditional knockout, DNA crosslinker sensitivity assay |
Nucleic acids research |
High |
25428364
|
| 2014 |
YY1 oligomers preferentially interact with RUVBL1 (rather than RUVBL2) and DNA binding by YY1 oligomers is enhanced in the presence of RuvBL1-RuvBL2. YY1 and the ATPase activity of RUVBL2 are required for RAD51 foci formation during homologous recombination. |
Co-immunoprecipitation, electron microscopy, in vitro DNA binding assay, functional HR assay (RAD51 foci) |
The Journal of biological chemistry |
Medium |
24990942
|
| 2014 |
RUVBL1 localizes to the cytoplasm in pancreatic cancer cells where it directly binds filamentous actin (F-actin), increases G-actin concentration in cell protrusions, promotes peripheral actin polymerization, and thereby drives formation of membrane protrusions to enhance cancer cell invasion. |
siRNA knockdown, co-immunoprecipitation, confocal microscopy (F-actin colocalization), motility/invasion assay |
International journal of oncology |
Medium |
24728183
|
| 2015 |
RUVBL1 localizes to structures of the mitotic spindle apparatus in anaphase-to-telophase transition, partially co-localizing with PLK1. PLK1 phosphorylates RUVBL1 (but not RUVBL2) in vitro, and they physically associate in vivo. siRNA knockdown of RuvBL proteins causes chromosome alignment and segregation defects, and the ATPase activity of RUVBL1 is indispensable for cell proliferation. |
Immunofluorescence microscopy, in vitro kinase assay (PLK1), co-immunoprecipitation, siRNA knockdown, ATPase-deficient mutant complementation assay |
PloS one |
Medium |
26201077
|
| 2015 |
A domain within the INO80 ATPase subunit (Ino80INS) stimulates Rvb1/2 ATPase activity 16-fold and promotes dodecamerization. Cryo-EM and mass spectrometry show Ino80INS binds asymmetrically at the dodecamerization interface, creating a conformationally flexible dodecamer that collapses into hexamers upon ATP addition, demonstrating chaperone-like cycling behavior. |
ATPase assay, cryo-EM, crosslinking mass spectrometry, integrative structural modeling |
Cell reports |
High |
28591576
|
| 2017 |
PRMT5 methylates RUVBL1 at arginine R205, which is required for TIP60-dependent mobilization of 53BP1 from DSBs and promotes homologous recombination. PRMT5-directed methylation of RUVBL1 is critically required for TIP60 acetyltransferase activity and histone H4K16 acetylation, which facilitates 53BP1 displacement. Methylation did not affect ATM activation. |
In vitro methyltransferase assay (PRMT5 on RUVBL1), mutant RUVBL1 (R205 site), TIP60 HAT activity assay, ChIP (H4K16Ac, 53BP1 foci), siRNA |
Molecular cell |
High |
28238654
|
| 2017 |
The R2TP/Prefoldin-like complex interacts with the U5 snRNP, mediated primarily by the uncharacterized factor ZNHIT2. ZNHIT2 directly binds RUVBL2's DII domain; disruption of ZNHIT2 or RUVBL2 expression impacts U5 snRNP protein composition, implicating RUVBL1/2 in U5 snRNP assembly. |
Affinity purification-MS (multi-target), co-immunoprecipitation, siRNA knockdown with snRNP composition analysis |
Nature communications |
Medium |
28561026
|
| 2017 |
Adenovirus E1A binds RUVBL1 via the C-terminus of E1A and is recruited to RUVBL1-regulated promoters in an interferon-dependent manner, suppressing interferon-stimulated gene transcriptional activation. Depletion of RUVBL1 impairs adenovirus growth but does not affect viral genome replication or S-phase induction. |
Co-immunoprecipitation (E1A-RUVBL1), ChIP, siRNA knockdown, viral growth assay, domain mapping |
Journal of virology |
Medium |
28122980
|
| 2018 |
RUVBL1 interacts with DNAAF1 and IFT88 (ciliary intraflagellar transport protein). Loss of RUVBL1 perturbs DNAAF1/IFT88 co-localization, and RUVBL1 orthologs show asymmetric left-sided distribution at the embryonic node and zebrafish Kupffer's vesicle. Conditional Ruvbl1 deletion in tubular epithelial cells causes renal failure with fewer ciliated cells; deletion in motile-ciliated cells causes hydrocephalus. Cilia of Ruvbl1-negative cells lack crucial ciliary proteins, consistent with cytoplasmic pre-assembly of ciliary complexes. |
Co-immunoprecipitation (RUVBL1-DNAAF1-IFT88), conditional mouse knockout (renal epithelium, motile cilia), immunofluorescence, zebrafish asymmetry assay |
Human molecular genetics / Experimental & molecular medicine |
High |
29228333 29959317
|
| 2019 |
The cryo-EM structure of the human R2TP co-chaperone complex (RUVBL1-RUVBL2-RPAP3-PIH1D1) reveals that binding of PIH1D1 to the DII domain of RUVBL2 induces conformational rearrangements that destabilize an N-terminal segment of RUVBL2 acting as a gatekeeper to nucleotide exchange, thereby regulating RUVBL2 ATPase activity. This DII-mediated nucleotide access mechanism is proposed to be general. |
Cryo-EM structure determination, biochemical validation of conformational changes |
Science advances |
High |
31049401
|
| 2019 |
CB-6644 is an allosteric small-molecule inhibitor of the RUVBL1/2 ATPase complex; drug-resistant clones carry mutations in RUVBL1 or RUVBL2, confirming on-target mechanism. Inhibition of RUVBL1/2 ATPase activity leads to cancer cell death and reduced tumor growth in AML and multiple myeloma xenograft models. |
In vitro ATPase inhibition assay, acquired resistance mutation mapping, xenograft tumor models |
ACS chemical biology |
High |
30640450
|
| 2019 |
RUVBL1/2 ATPase activity is necessary for maturation/dissociation of the PAQosome (large RUVBL1/2-dependent multiprotein complex) and for DNA replication; its inhibition causes S-phase arrest and replication catastrophe in cancer cells. |
RUVBL1/2 ATPase inhibitor treatment, PAQosome complex analysis, S-phase flow cytometry, replication assay |
Cell chemical biology |
Medium |
31883965
|
| 2019 |
RUVBL1 promotes the RAF/MEK/ERK pathway by binding C-RAF and inhibiting phosphorylation of C-RAF at serine 259, thereby activating the pathway to promote lung cancer cell proliferation and invasion. |
Co-immunoprecipitation (RUVBL1-CRAF), immunoblot for pS259-CRAF, RUVBL1 knockout (cell proliferation/invasion assay), xenograft model |
Biochemical and biophysical research communications |
Medium |
29545175
|
| 2020 |
RUVBL1-RUVBL2 complex controls assembly and composition of the gamma-tubulin ring complex (γTuRC) in human cells. RUVBL1/2 interacts with γTuRC subcomplexes but is absent from fully assembled γTuRC. Purified, RUVBL1/2-assembled recombinant γTuRC has microtubule nucleation activity and resembles native γTuRC by cryo-EM (~4.0 Å). |
siRNA knockdown (γTuRC assembly), heterologous coexpression reconstitution, cryo-EM structure (~4.0 Å), co-immunoprecipitation, microtubule nucleation assay |
Science advances |
High |
33355144
|
| 2020 |
Cryo-EM reveals that DHX34, an RNA helicase regulating NMD initiation, directly interacts with RUVBL1-RUVBL2 in vitro and in cells. DHX34 binding induces extensive conformational changes in N-termini of every RUVBL2 subunit, stabilizing a conformation that cannot bind nucleotide, downregulating RUVBL2 ATP hydrolysis. ATPase-deficient mutants show DHX34 acts exclusively on RUVBL2 subunits. |
Cryo-EM structure, in vitro binding assay, co-immunoprecipitation, ATPase-deficient mutant analysis |
eLife |
High |
33205750
|
| 2020 |
Both excess and depletion of RUVBL1 impede DNA replication through transcription-dependent mechanisms. RUVBL1 overexpression increases c-Myc-dependent RNAPII pause release and transcription; RUVBL1 depletion increases Rpb1 ubiquitination and reduces RNAP II mobility, causing stalled RNAPII. Both states result in replication-transcription interference. |
siRNA knockdown, RUVBL1 overexpression, pSer2 CTD immunoblot, Rpb1 ubiquitination assay, FRAP, replication fork rate measurement |
The international journal of biochemistry & cell biology |
Medium |
32846207
|
| 2021 |
NOPCHAP1 (C12ORF45) acts as a PAQosome cofactor that bridges NOP58 to the PAQosome by making direct physical interactions with the CC-NOP domain of NOP58 and domain II of RUVBL1/2 AAA+ ATPases. NOPCHAP1 interaction with RUVBL1/2 is disrupted upon ATP binding, suggesting a nucleotide-regulated client-loading mechanism for C/D snoRNP biogenesis. |
Co-immunoprecipitation, in vitro direct binding assay, ATP competition assay, NOP58 KO cell analysis, proteomic pulldown |
Nucleic acids research |
High |
33367824
|
| 2021 |
RUVBL1 interacts with SMCHD1 and is present at D4Z4 chromatin; loss of RUVBL1 further derepresses DUX4 in FSHD myocytes, placing RUVBL1 in a SMCHD1-dependent chromatin repression pathway at the D4Z4 locus. |
Quantitative proteomics (SMCHD1 interactome), ChIP, siRNA knockdown, DUX4 derepression assay |
Scientific reports |
Medium |
34880314
|
| 2022 |
Rvb1/Rvb2 are enriched at promoters and mRNAs of alternative glucose metabolism genes during starvation. Engineered Rvb1/Rvb2 tethering to mRNAs is sufficient to sequester those mRNAs into mRNP granules, repress their translation, and drive further transcriptional upregulation of target genes, demonstrating coupling of transcription, mRNA localization, and translation. |
ChIP, RNA immunoprecipitation, mRNA tethering (engineered binding), stress granule imaging, ribosome profiling, genetic depletion |
eLife |
Medium |
36107469
|
| 2022 |
LINC00839 (lncRNA) recruits RUVBL1 to the Tip60 complex and increases its acetyltransferase activity; the complex is guided to the NRF1 promoter and promotes H4K5 and H4K8 acetylation to upregulate NRF1 expression. |
Co-immunoprecipitation (LINC00839-RUVBL1-TIP60), ChIP (H4K5Ac, H4K8Ac at NRF1 promoter), siRNA/shRNA knockdown, reporter assay |
EMBO reports |
Medium |
35876654
|
| 2022 |
RUVBL1/2 inhibition significantly reduces histone H3K4me3 at the Nos2 and Il6 promoters and diminishes NF-κB recruitment to corresponding enhancers, demonstrating that RUVBL1/2 regulate macrophage pro-inflammatory gene expression through epigenetic H3K4 trimethylation. |
siRNA knockdown, RUVBL1/2 pharmacological inhibition, ChIP (H3K4me3, NF-κB), transcriptome analysis, functional NO production assay |
Frontiers in immunology |
Medium |
34276666
|
| 2022 |
DPCD directly interacts with RUVBL1 and RUVBL2 in vitro and in cells, predominantly via DII domains of RUVBL1/2. DPCD binding disrupts the dodecameric state of the RUVBL1/2 complex. |
Co-immunoprecipitation (in vivo), in vitro direct binding assay, SAXS, structural mass spectrometry, electron microscopy |
Journal of molecular biology |
High |
35901867
|
| 2023 |
GART methylates RUVBL1 at K7, enhancing RUVBL1 protein stability. This stabilization aberrantly activates the Wnt/β-catenin signaling pathway to induce tumor stemness in colorectal cancer. |
In vitro methyltransferase assay (GART on RUVBL1 K7), site-directed mutagenesis (E948 active site), co-immunoprecipitation, protein stability assay, β-catenin pathway reporter |
Advanced science |
Medium |
37439412
|
| 2023 |
RUVBL1 controls MYC chromatin binding and modulates MYC-driven EEF1A1 expression and protein synthesis. A high-density CRISPR gene body scan identified the MYC-interacting residue(s) in RUVBL1 critical for this function. |
CRISPR screen (gene body scan), ChIP (MYC binding), RUVBL1 suppression (shRNA/CRISPR), protein synthesis assay |
Advanced science |
Medium |
37075745
|
| 2024 |
DTL ubiquitinates RUVBL1 and facilitates RUVBL1 binding to RUVBL2 and β-catenin. Ubiquitinated RUVBL1 promotes transcriptional regulation of NHEJ repair pathway genes via the RUVBL1/2–β-catenin complex, while attenuating TIP60-mediated H4K16 acetylation and HR repair, thereby enhancing radioresistance. |
Co-immunoprecipitation (DTL-RUVBL1, RUVBL1-RUVBL2-β-catenin), ubiquitination assay, ChIP (NHEJ gene promoters, H4K16Ac), siRNA/knockdown, in vitro and in vivo radioresistance assays |
Cell death & disease |
Medium |
38609375
|
| 2024 |
RUVBL1 is required for MYC to establish oncogenic and immunoevasive gene expression in pancreatic ductal adenocarcinoma (PDAC). Degradation of RUVBL1 (auxin-degron system) arrests cancer but not untransformed cells and causes complete tumor regression in mice, preceded by immune cell infiltration. |
shRNA library screen (in vitro and in vivo), auxin-degron targeted degradation, gene expression analysis, in vivo PDAC mouse tumor model |
Gut |
High |
38821858
|
| 2024 |
RUVBL1 promotes enzalutamide resistance in prostate cancer by localizing to the cytoplasm upon enzalutamide treatment, enhancing recruitment of CRAF to plexin A1 (PLXNA1), and activating the downstream MAPK pathway. |
Co-immunoprecipitation (RUVBL1-CRAF-PLXNA1), subcellular fractionation (cytoplasmic RUVBL1), siRNA/CB-6644 inhibition, xenograft model |
Oncogene |
Medium |
35508542
|
| 2024 |
RUVBL1/2 reciprocally interact with YTHDF1 at 40S translation initiation complexes (identified by Co-IP and mass spectrometry). RUVBL1/2 loss stalls YTHDF1-driven oncogenic translation and nascent protein biosynthesis; ribosome sequencing shows impaired MAPK, RAS, and PI3K-AKT signaling translation upon RUVBL1/2 depletion. |
Co-immunoprecipitation, mass spectrometry, ribosome sequencing, siRNA knockdown, polysome profiling |
Cancer research |
High |
38900944
|