{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Libing Song"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0003550000"],"submitter_email":["songlb@sysucc.org.cn"],"submitter_affiliation":["Sun Yat-sen University Cancer Center"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["Nicotine addiction and the occurrence of lymph node spread are two major significant factors associated with esophageal cancer's poor prognosis; however, nicotine's role in inducing lymphatic metastasis of esophageal cancer remains unclear. Here we show that OTU domain-containing protein 3 (OTUD3) is downregulated by nicotine and correlates with poor prognosis in heavy-smoking esophageal cancer patients. OTUD3 directly interacts with ZFP36 ring finger protein (ZFP36) and stabilizes it by inhibiting FBXW7-mediated K48-linked polyubiquitination. ZFP36 binds with the VEGF-C 3-'UTR and recruits the RNA degrading complex to induce its rapid mRNA decay. Downregulation of OTUD3 and ZFP36 is essential for nicotine-induced VEGF-C production and lymphatic metastasis in esophageal cancer. This study establishes that the OTUD3/ZFP36/VEGF-C axis plays a vital role in nicotine addiction-induced lymphatic metastasis, suggesting that OTUD3 may serve as a prognostic marker, and induction of the VEGF-C mRNA decay might be a potential therapeutic strategy against human esophageal cancer."],"pubmed_title":["Nicotine-mediated OTUD3 downregulation inhibits VEGF-C mRNA decay to promote lymphatic metastasis of human esophageal cancer."],"pubmed_authors":["Wang Meng M, Li Yue Y, Xiao Yunyun Y, Yang Muwen M, Chen Jinxin J, Jian Yunting Y, Chen Xin X, Shi Dongni D, Chen Xiangfu X, Ouyang Ying Y, Kong Lingzhi L, Huang Xinjian X, Bai Jiewen J, Lin Chuyong C, Song Libing L"],"additional_accession":[]},"is_claimable":false,"name":"Identification of OTUD3 interactors in esophageal cancer cell line","description":"Immunoprecipitation of OTUD3 interacting proteins was subjected to SDS-PAGE, silver-stained, and identified by mass spectrometry (MS).","dates":{"publication":"Sun Sep 26 00:00:00 BST 2021"},"accession":"PXD028751","cross_references":{"TAXONOMY":["9606"],"pubmed":["34853315"]}}