{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/FBXO28-KM.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/IAA-ISOTPABPP-KM.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-KM-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/IAA-ISOTPABPP-KM.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-KM-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-KM-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-DMSO-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-DMSO-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/FBXO28-KM.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-DMSO-2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/Homo_sapiens_uniprot_canonical_20395_entries_20210516.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/FBXO28.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067337/COIP-UP000005640_9606.fasta"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pharmlzq@jnu.edu.cn"],"submitter":["Jianxiong Deng"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067337"],"sample_protocol":["1. Co-IP/MS experiment NCI-H23 cells were used in this study. Cells were incubated with MG132 (4 μM) for 6 h, and then incubated with DJX-A-KM (40 nM) or DMSO for 8 h. Cells were suspended and lysed in NP-40 lysis buffer supplemented with complete protease inhibitor cocktail. The cell suspension was incubated on ice for 1 h. Subsequently, the mixture was centrifuged at 3,000 g for 10 min at 4 °C. The protein concentration was determined by BCA protein assay. For immunoprecipitation, KRAS antibody was added to the protein lysates and rotated at 4 °C for 4 h. 50 µL of protein A/G Agarose (Beyotime, P2012) was then added to each group of samples for enrichment. The Agarose was then washed four times with precooled PBS. Subsequently, the sample was resuspended in 500 μL ammonium bicarbonate (50 mM) and incubated with 25 μL of 200 mM DTT for 30 min at 37℃, followed by 25 μL of 400 mM IAA for 1 h at room temperature in the dark. Dilute the sample with 500 μL ammonium bicarbonate and digest overnight at 37°C with 5 μg trypsin. The peptides were desalted by C18 column and then analyzed by LC-MS/MS. 2.Cysteine-directed activity-based protein profiling (ABPP) To determine the specific site of DJX-A-KM with the E3 ubiquitin ligase FBXO28 during KRASG12C degradation in living cells, we used cysteine-directed activity-based protein profiling (ABPP) to quantify cysteine modified by DJX-A-KM, iodoacetamide (lAA) alkyne probe was used as a tool probe. NCI-H23 cells were grown to 80-90% in 10 cm dishes under conditions described above. The cells were pre-treated with MG-132 (4 µM) for 2 h, then treated with DMSO or DJX-A-KM (200 nM) for 3 h, followed by cell lysis with PBS buffer and the resulting proteome was divided into equal parts. The cell lysates were treated with the IA-alkyne (100 µM, 2 h, 37 °C), respectively. After trypsin digestion, different groups were treated with H/L UV cleavable biotin-Ns for the corresponding click reactions. The resulting light and heavy protein groups were combined and affinity purified. The peptides were released after UV irradiation sand subsequently analyzed by LC-MS/MS. 3.Modification site analysis of recombinant FBXO28 protein with DJX-A-KM Recombinant FBXO28 protein was diluted to 1 mg/mL with PBS and was incubated with the probe DJX-A-KM (final concentration is 5 μM) at 37 ℃ for 5 h. The resulting mixture was transferred to the pre-activated ultrafiltration membrane spin column, followed by washing with PBS (3 times), 1 x TEAB (2 times), and finally reconstituted with TEAB. The reaction solution was resuspended with 1 M DTT solution (final concentration is 10 mM), and incubated at 37 ℃ for 30 min. For alkylation, 1 M IAA aqueous solution (final concentration is 20 mM) was added followed by incubation for 30 min at rt. in dark. After alkylation, DTT aqueous solution (final concentration is 10mM) was added. The samples were washed with PBS and TEAB buffer 6 times, respectively, and reconstituted with TEAB. For the digestion, 1 μL trypsin (1 μg/μL) was added in a ratio of 1:50 (amount of protein). The reaction was incubated at room temperature overnight. After that, the filtrates were collected by centrifugation and washed twice with ultrapure water. The washing buffer were combined and then desalted by C18 column. After evaporation, the samples were analyzed by LC-MS/MS"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The protein identification raw data were processed by using MaxQuant and processed as per default workflow. MS tolerance is 4.5 ppm, and MS/MS tolerance is 20 ppm. Reversed database searches were used to evaluate false discovery rate (FDR) of peptide and protein identifications. Two missed cleavage sites of trypsin were allowed, compound modification was set as variable modifications. The FDR of both peptide identification and protein identification were set to be 1%. The options of “second peptides”, “match between runs” and “dependent peptides” were used. Label-free quantification was used to quantify the difference between different samples."],"omics_type":["Proteomics"],"labhead":["zhengqiu li"],"instrument_platform":[""],"labhead_affiliation":["JINAN UNIVERSITY"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["1347350344@qq.com"],"publication":["10.1038/S41467-026-71093-9"],"submitter_affiliation":["JINAN UNIVERSITY"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Small-molecule degraders for oncogenic KRASG12C and pan-KRAS mutations","description":"KRAS, one of the most frequently mutated oncogenes in cancer, has long posed a formidable therapeutic challenge due to the difficulty of directly inhibiting its activity. A major breakthrough emerged with the development of covalent, allele-specific in-hibitors targeting KRASG12C, such as sotorasib. However, the clinical utility of these inhibitors is frequently limited by the rapid development of acquired resistance. Targeted protein degradation (TPD) has emerged as an effective approach with the potential to overcome drug resistance, but it has been mostly restricted to large-size PROTACs. In this study, we present the first small-molecule KRASG12C degrader, DJX-A-KM, designed by integrating a simple acrylamide warhead into the hydrophilic moiety of the MRTX849 scaffold. DJX-A-KM induces rapid, robust, and sustained degradation of KRASG12C in both cellular and animal models (DC50: 2 nM; Dmax: 98%; 60h durability), demonstrating superior pharmaceutical properties to PROTACs. Mechanistic investigations revealed that degradation is mediated by the ubiquitin-proteasome system, facilitated by covalent engagement with a new E3 ligase, FBXO28, at cysteine 98 through the acrylamide warhead. Antiproliferation assays demonstrated its potent in-hibitory effects across multiple KRASG12C-mutant cancer models, with in vivo studies confirming significant tumor growth sup-pression mediated by targeted KRASG12C degradation. Notably, this chemical strategy extends beyond KRASG12C, offering a blueprint for developing pan-KRAS degraders against a broader spectrum of KRAS mutations. To our knowledge, this study reports the first small-molecule degrader that recruits FBXO28 as an E3 ligase, employing a novel dual covalent strategy to achieve the highest targeted degradation of KRASG12C thus far. Additionally, it represents the first small-molecule pan-KRAS degrader and provides a feasible approach for exploring new E3 ligases in targeted protein degradation 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