{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shControl_N3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shControl_N1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shCbll1_N1.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shCbll1_N3.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shCbll1_N2.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD069248/Tumorspheres_shControl_N2.d.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["angelica.figueroa.conde-valvis@sergas.es"],"submitter":["María Pereira Blanco"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Colon Cancer"],"software":[""],"submitter_keywords":["colon cancer.","cancer stem cell","E3 ubiquitin-ligase hakai","wnt/β-catenin pathway","lrp4","E3 ubiquitin-ligase hakai; lrp4; wnt/β-catenin pathway; cancer stem cell; colon cancer."],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069248"],"tissue":["Epithelial Cell","Colon"],"sample_protocol":["Equal amounts of each sample (approximately 10 µg) were reduced with 2 µL of 10 mM dithiothreitol (DTT) for 1 h at 37 °C under agitation. Subsequently, alkylation with 50 mM iodoacetamide (IAA) was performed in the dark for 45 minutes at room temperature. After incubation, ammonium bicarbonate was added to each sample to achieve a final volume of 80 µL with the aim of diluting urea to allow trypsin to act. Following pH adjustment, the samples were digested with sequencing grade-modified trypsin (Promega) at a 1:30 enzyme-to-substrate ratio. After 17 h of digestion at 37 °C under agitation, samples were acidified with 10% trifluoroacetic acid (TFA) to ~pH 3 to stop the reaction and then concentrated under speed-vacuum (SpeedVac, Thermo Fisher Scientific) and sonicated for 3 minutes. Subsequently, the digested peptides were desalted using in-house made stage tips (3M Empore SPE-C18 disk, 47 mm, Sigma-Aldrich). Stage tips are devices used for the purification and concentration of peptides before analysis by mass spectrometry. They consist of small tips filled with ion exchange resins or reverse-phase chromatography resins that allow for selective retention of peptides while removing contaminants, improving sensitivity and result quality. The tips were previously activated with methanol, then with a solution of 80% hydrogen cyanide (HCN) + 0.5% TFA, and finally with 0.5% TFA. After passing the sample through the tips, two washes with formic acid (FA) were performed, and then peptide elution was carried out with a solution of 30 µL of 80% HCN + 0.5% TFA in water. Finally, samples were dried under SpeedVac and stored at -80 °C for subsequent mass spectrometry analysis."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw data files were analyzed to obtain protein identifications using MaxQuant, and LFQAnalyst was used for the analysis of Label-Free Quantitative (LFQ) proteomic data sets. LFQ is a method used in proteomics to quantify proteins in a sample without the need for labelling them with chemical markers; instead, it relies on comparing mass spectrometry signals across different samples. Statistical analyses were carried out with an in-house R script using the MaxQuant “proteinGroup.txt” as the primary input file in conjunction with an experimental design text file, which describes conditions and replicates. Contaminant proteins, reverse sequences, proteins identified “only by site” or with “only by a single peptide” were removed. LFQ intensity data were converted to a log2 scale, and replicates were grouped by conditions based on the information provided in the “experimental design.txt” file. Missing values were imputed using the “Missing not At Random” (MNAR) method, which uses random draws from a Gaussian distribution left-shifted by 1.8 standard deviations with a width of 0.3. To determine significantly regulated proteins between conditions, a cutoff of an adjusted p-value of 0.05 (Benjamini−Hochberg method), a fold change of 1.5, and a requirement of at least two peptides were applied. Finally, the Uniprot database (https://www.uniprot.org/) was utilized to analyze the functional descriptions of significantly regulated proteins. Interactive network analysis was conducted using STRING (Search Tool for the Retrieval of Interacting Genes, http://string-db.org) and TIMER 2.0 (http://timer.cistrome.org)."],"omics_type":["Proteomics"],"labhead":["Angélica Figueroa"],"instrument_platform":[""],"labhead_affiliation":["Epithelial Plasticity and Metastasis Group, Instituto de Investigación Biomédica de A Coruña (INIBIC)"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["maria.pereira.blanco@sergas.es"],"submitter_affiliation":["Epithelial Plasticity and Metastasis Group\nInstituto de Investigación Biomédica A Coruña (INIBIC)"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"E3 ubiquitin-ligase Hakai induces LRP4 degradation and regulates Wnt/β-catenin signalling in colorectal cancer cells","description":"The epithelial-mesenchymal transition (EMT) is closely linked to the acquisition of cancer stem cell (CSC) properties, which contribute to treatment resistance and metastasis. This study investigates the role of the E3 ubiquitin-ligase Hakai, the first identified post-translational regulator of E-cadherin stability, in promoting CSC traits in colorectal cancer (CRC). To examine Hakai’s involvement in CSC regulation, we used an inducible shRNA in a HT29 cells. Under conditions that promote CSC characteristics, we silenced Hakai and evaluated tumoursphere formation and CSC marker expression. Proteomic and bioinformatic analyses were performed to identify Hakai-regulated proteins in tumoursphere cultures. Additionally, Western blot, RT-qPCR, co-immunoprecipitation, immunofluorescence and TOPFlash assays were employed to study CSC-related protein regulation in response to Hakai expression. Furthermore, we assessed the impact of Hakin-1, the pharmacological inhibitor specifically targeting Hakai’s HYB domain responsible for its E3 ubiquitin-ligase activity, on tumoursphere properties. Hakai silencing significantly reduced tumoursphere size and number accompanied by decreased expression of CSC markers and Wnt target genes. CSC-related proteins regulated by Hakai were identified, including LRP4, a negative regulator of Wnt/β-catenin pathway. Hakai interacts with LRP4, promoting its ubiquitination and degradation. Moreover, Hakai overexpression induces hyperactivation of Wnt/β-catenin sand disrupts LRP4’s inhibitory effect. Treatment with Hakin-1 effectively inhibited self-renewal and promoted differentiation within tumourspheres. These findings suggest that Hakai promotes CSCs properties by hyperactivation of the Wnt/β-catenin pathway via LRP4-mediated modulation. Additionally, Hakin-1 emerges as a promising therapeutic agent targeting CSCs by enhancing differentiation and attenuating Wnt/β-catenin activity, highlighting Hakai as a potential target for improving CSC 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