{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045485/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045485/RE802ELQ_IP15_2.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045485/txt.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045485/RE802ELQ_IP15_1.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["2427887530@qq.com"],"submitter":["Xinyu Guo"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Immunotherapy","Ptm","Hcc","Pd-l1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045485"],"tissue":["Cell Culture"],"sample_protocol":["Cell samples were collected and lysed in lysis buffer (20 mM HEPES, pH 7.4, 150 mM NaCl, 1mM EDTA, 2mM MgCl2 and 0.1% Triton X-100) supplemented with a protease inhibitor cocktail. After the cell lysates were collected and centrifugated, incubated with indicated magnetic beads at 4 °C with gentle rotation for 4h. The magnetic beads were incubated with the indicated antibodies overnight in advance. After washing three times with wash buffer.Then, the immunoprecipitated samples after elution by glycine (0.1M, pH 1.4) and neutralization by HEPES were analyzed by liquid chromatography-tandem mass spectrometry. The peptides were dissolved in mobile phase A by liquid chromatography and separated by EASY-nLC 1200 ultra-high performance liquid phase system. Mobile phase A is an aqueous solution containing 0.1% formic acid and 2% acetonitrile. Mobile phase B is an aqueous solution containing 0.1% formic acid and 90% acetonitrile. Liquid phase gradient setting: 0-68 min, 6%~23%B; 68.0-82.0 min, 23%-32% B; 82.0 - 86.0 min, 32%~80%B; 86.0-90.0 min, 80%B, the flow rate maintained at 500 nL/min. The peptides were separated by an ultra-high performance liquid phase system and ionized into an NSI ion source, and then analyzed by Orbitrap Exploris™ 480 (ThermoFisher Scientific) mass spectrometry. The ion source voltage was set to 2.3 kV and the FAIMS compensation voltage (CV) was set to -. The peptide parent ions and their secondary fragments were detected and analyzed using high-resolution Orbitrap. The scanning range of primary mass spectrometry is set to 400-1200m /z, and the scanning resolution is set to 60000. The scanning range of the secondary mass spectrometry is fixed at 110 m/z, the secondary scanning resolution is set to 15000, and the TurboTMT is set to Off. The data acquisition mode uses data-dependent scanning (DDA) procedure, that is, the first 25 peptide parent ions with the highest signal intensity are selected to enter the HCD collision pool in sequence after the primary scanning, and the fragmentation energy of 27% is used for fragmentation. In order to improve the effective utilization of mass spectrum, the automatic gain control (AGC) is set to 1E5, the signal threshold is set to 5E5 ions/s, the maximum injection time is set to Auto, and the dynamic exclusion time of series mass spectrum scanning is set to 20 s to avoid repeated scanning of parent ions."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Database retrieval is a complex computational process, which requires the use of professional mass spectrum data analysis software for data analysis. The original mass spectrometry data were imported into the database search software, and the corresponding analysis parameters were set according to the experimental scheme. Maxquant (v1.6.15.0) was used to retrieve secondary mass spectrometry data in this experiment. Search parameter Settings: The database was Mus_musculus_10090_SP_20230103.fasta (17132 sequences), the anti-database was added to calculate the false positive rate (FDR) caused by random matching, and the common contamination database was added to the database to eliminate the influence of contaminated proteins in the identification results. The enzyme digestion method was set as Trypsin/P.  The number of missing cuts is set to 4; The minimum length of the peptide was set to 7 amino acid residues. The maximum number of peptide modifications was set to 5. The mass error tolerance for primary parent ions was set at 20 ppm and 4.5 ppm respectively for first search and main search, and 20 ppm for secondary fragment ions. The cysteine alkylated Carbamidomethyl (C) was set as a fixed modification, which was modified to oxidation of methionine, n-terminal acetylation of protein, deamidation (NQ), threonine, serine, tyrosine phosphorylation, lysine ubiquitination (Gly-Gly), and lysine acetylation. The FDR for protein identification and PSM identification was set at 1%."],"omics_type":["Proteomics"],"labhead":["Xinyu Guo"],"instrument_platform":[""],"labhead_affiliation":["The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China; The First Affiliated Hospital of Harbin Medical University"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["39690246 Guo X, Cui T, Sun L, Fu Y, Cheng C, Wu C, Zhu Y, Liang S, Liu Y, Zhou S, Li X, Ji C, Ma K, Zhang N, Chu Q, Xing C, Deng S, Wang J, Liu Y, Liu L. A STT3A-dependent PD-L1 glycosylation modification mediated by GMPS drives tumor immune evasion in hepatocellular carcinoma. Cell Death Differ. 2025 32(5):944-958 10.1038/s41418-024-01432-0"],"submitter_mail":["2427887530@qq.com"],"submitter_affiliation":["The First Affiliated Hospital of Harbin Medical University"],"submitter_country":["China"],"pubmed_abstract":["Hepatocellular carcinoma (HCC) is a malignant tumor characterized by rapid progression. To explore the regulatory mechanism of rapid tumor growth and metastasis, we conducted proteomic and scRNA-Seq analyses on advanced HCC tissues and identified a significant molecule, guanine monophosphate synthase (GMPS), closely associated with the immune evasion in HCC. We analyzed the immune microenvironment characteristics remodeled by GMPS using scRNA-Seq and found GMPS induced tumor immune evasion in HCC by impairing the tumor-killing function of CD8 <sup>+</sup> T cells. Further investigation revealed that GMPS increased PD-L1 expression by regulating its ubiquitination and glycosylation modification. Mechanistically, GMPS enhanced the bond between PD-L1 and the catalytic subunit STT3A of oligosaccharyltransferase (OST) by acting as an additional module connecting the Sec61 channel complex and STT3A, which aided in the translocation and modification of nascent peptides. Increased PD-L1 impaired the tumor-killing function of CD8 <sup>+</sup> T cells, leading to the immune evasion. Importantly, targeting GMPS with angustmycin A, an inhibitor of GMPS activity, significantly suppressed PD-L1 expression and tumor growth in HCC, which also increased the sensitivity to anti-CTLA-4 immunotherapy. These findings suggested the potential of targeting GMPS as a promising therapeutic approach for HCC."],"pubmed_title":["A STT3A-dependent PD-L1 glycosylation modification mediated by GMPS drives tumor immune evasion in hepatocellular carcinoma."],"pubmed_authors":["Guo Xinyu X, Cui Tianming T, Sun Linmao L, Fu Yumin Y, Cheng Cheng C, Wu Chenghui C, Zhu Yitong Y, Liang Shuhang S, Liu Yufeng Y, Zhou Shuo S, Li Xianying X, Ji Changyong C, Ma Kun K, Zhang Ning N, Chu Qi Q, Xing Changjian C, Deng Shumin S, Wang Jiabei J, Liu Yao Y, Liu Lianxin L"],"additional_accession":[]},"is_claimable":false,"name":"GMPS promoting tumor immune evasion by regulating the glycosylation modification of PD-L1","description":"Hepatocellular carcinoma (HCC) is a malignant tumor characterized by rapid progression, whose development is attributed to severe immune evasion. Here, we conducted proteomic and scRNA-Seq analysis on advanced HCC tissues and identified a significant molecule, Guanine monophosphate synthase (GMPS). We found that GMPS was closely associated with the immune evasion of HCC. Further investigation revealed that GMPS increased PD-L1 expression by regulating its ubiquitination and glycosylation modification. Mechanistically, GMPS enhanced the bond between PD-L1 and the catalytic subunit STT3A of oligosaccharyltransferase (OST) through acting as an additional module connecting the Sec61 channel complex and STT3A, which aided in the translocation and modification of nascent peptides. The increased PD-L1 impaired the tumor-killing function of CD8+ T cells, ultimately leading to immune evasion. Importantly, targeting GMPS with angustmycin A, an inhibitor of GMPS activity, significantly suppressed PD-L1 expression and tumor growth in HCC, which also increased sensitivity to anti-CTLA-4 immunotherapy. These findings suggested the potential of targeting GMPS as a promising therapeutic approach for 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