{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/Maxquant_search.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep3_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/IgG_rep2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067138/AR_rep3_2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["echeung@um.edu.mo"],"submitter":["Cuiting Zhang"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Prostate Cancer"],"software":[""],"submitter_keywords":["Castration-resistant prostate cancer","Immunosuppression","Ar coregulator","Gnl3"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067138"],"tissue":["Malignant Cell","Cell Culture"],"sample_protocol":["Culture 2 × 10^7 C4-2B cells in 15 cm dishes with hormone-deprived medium for 72 hours. Then, cells were treated with 100 nM DHT for 2 hours and crosslinked with 1% methanol-free formaldehyde at room temperature for 10 minutes. Lyse the cells and 10 μg anti-AR or rabbit IgG antibody pre-coated with protein G Dynabeads was applied for immunoprecipitation. Bound proteins on beads were extracted for 10 minutes in a denaturing buffer (0.02 M Tris-HCl, pH 6.9, 2% SDS, 0.1 M dithiothreitol)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein digestion was performed with trypsin employing the filter-aided sample preparation (FASP) protocol. Next, purify the tryptic peptides using C18 ZipTips following the manufacturer’s protocol. Following digestion and purification, the peptides were dried using a SpeedVac concentrator to remove residual solvents. The dried peptides were then carefully reconstituted in a solution containing 0.1% formic acid and 5% acetonitrile (ACN) to enhance solubility and ensure compatibility with LC-MS/MS analysis. Peptide separation was carried out on an EASY-Spray™ liquid chromatography column (75 μm × 50 cm, 2 μm, 100 Å pore size). Then, elute the peptides over a 65-minute gradient ranging from 5% to 35% ACN in 0.1% formic acid, allowing for efficient resolution of complex peptide mixtures. The eluted peptides were subsequently analyzed in data-dependent acquisition (DDA) mode and introduced into a Q Exactive mass spectrometer (Thermo Fisher Scientific). Full MS scans were acquired over a mass-to-charge (m/z) range of 400-2,500 at a resolution of 70,000 (full width at half maximum, FWHM), ensuring high mass accuracy and sensitivity for peptide detection. The top 20 most intense precursor ions from each scan were automatically selected for fragmentation via higher-energy collisional dissociation (HCD) with a normalized collision energy (NCE) of 25. Fragment ion (MS/MS) spectra were subsequently recorded at a resolution of 17,500 (FWHM), enabling precise identification of peptide sequences.  Data were processed using MaxQuant (v1.5.3.17),  with database searching performed against the reviewed UniProt human protein database. Proteins were identified based on the detection of at least two unique peptides per protein. Stringent filtering criteria were applied, with peptide-spectrum match (PSM), dependent peptide, and protein false discovery rates (FDRs) all controlled at 0.01. For quantitative analysis, label-free quantification (LFQ) intensities were calculated using unique and razor peptides."],"omics_type":["Proteomics"],"labhead":["Edwin Cheung"],"instrument_platform":[""],"labhead_affiliation":["Faculty of Health Sciences, University of Macau, Taipa, Macau, China"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41772945 Zhang C, Cheong TL, Narwade N, Dong D, Deng M, Miao Z, Ding Z, Li W, Lei KMK, Wei GH, Poon TCW, Deng CX, Cheung E. GNL3 Orchestrates AR Transcriptional Programs to Drive Castration-Resistant Prostate Cancer and Immune Evasion. Adv Sci (Weinh). 2026 13(26):e16411 10.1002/advs.202516411"],"submitter_mail":["cuiting-zhang@outlook.com"],"submitter_affiliation":["University of Macau"],"submitter_country":["China"],"pubmed_abstract":["Androgen receptor (AR) signaling is a primary oncogenic driver of castration-resistant prostate cancer (CRPC), yet the mechanism remains incompletely understood. Through proteomic profiling of CRPC and primary PCa cells, we identify G Protein Nucleolar 3 (GNL3) as a novel AR coregulator. GNL3 physically interacts with AR, enhances its chromatin occupancy, and directly coactivates transcriptional programs that promote cell proliferation, including NEK2 and CDC20. Concurrently, GNL3 functions as a corepressor of immune-responsive genes such as CXCL10 and TAP1 via class I histone deacetylases (HDACs), thereby facilitating CD8+ T cell elimination and establishing an immunosuppressive tumor microenvironment. GNL3 expression and AR-GNL3 complex formation progressively increase from normal prostate to CRPC and correlate with poor clinical outcomes. Functionally, GNL3 knockdown sensitizes CRPC cells to AR antagonists and impairs tumor growth and metastasis. Furthermore, we demonstrate that combinatorial inhibition of NEK2, class I HDACs, and AR signaling can be a potential therapeutic strategy for CRPC. Overall, these findings establish GNL3 as a dual-function AR coregulator and therapeutic target, providing mechanistic insights into transcriptional regulation and immune evasion in advanced PCa."],"pubmed_title":["GNL3 Orchestrates AR Transcriptional Programs to Drive Castration-Resistant Prostate Cancer and Immune Evasion."],"pubmed_authors":["Zhang Cuiting C, Cheong Tin Long TL, Narwade Nitin N, Dong Dandan D, Deng Mokan M, Miao Zhengqiang Z, Ding Zhaoqiang Z, Li Wenchao W, Lei Kate Man Kei KMK, Wei Gong-Hong GH, Poon Terence Chuen Wai TCW, Deng Chu-Xia CX, Cheung Edwin E"],"additional_accession":[]},"is_claimable":false,"name":"GNL3 orchestrates AR transcriptional programs to drive castration-resistant prostate cancer and immune evasion","description":"Androgen receptor (AR) signaling is a primary oncogenic driver of castration-resistant prostate cancer (CRPC), yet the mechanism remains incompletely understood. Dysregulation of the AR co-regulatory network has emerged as a key driver of castration resistance. To identify AR-interacting proteins linked to CRPC progression, we performed proteomics-based rapid immunoprecipitation of endogenous proteins (RIME) analysis targeting AR in the CRPC cell line 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