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This study investigates how Ubiquitin carboxyl-terminal hydrolase L3 (UCHL3) regulates the deubiquitination and stabilization of eukaryotic translation elongation factor 1 alpha 1 (EEF1A1). Using clinical tissues and molecular assays, it characterizes the UCHL3–EEF1A1 regulatory axis and evaluates its effects on malignant migration, stemness, drug resistance, and tumor behavior in nude mouse models.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/uchl3-promotes-hepatocellular-carcinoma-progression-by-stabilizing-eef1a1-through-deubiquitination/333510/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/uchl3-promotes-hepatocellular-carcinoma-progression-by-stabilizing-eef1a1-through-deubiquitination/333510.png","ImageObject",300,407,{"name":92,"@type":93},"Violet","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-31","2026-09-21",true,{"@type":102,"interactionType":103,"userInteractionCount":34},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What biological mechanism does the paper propose between UCHL3 and EEF1A1 in HCC?","Question",{"text":112,"@type":113},"The study proposes that UCHL3 binds to EEF1A1 at a lysine site, reduces EEF1A1 ubiquitination, and stabilizes EEF1A1 through deubiquitination.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"How was the UCHL3–EEF1A1 relationship validated in this research?",{"text":117,"@type":113},"It was validated using clinical tissue samples and multiple molecular approaches including RT-qPCR, Western blotting, co-immunoprecipitation, immunofluorescence, ubiquitin detection, and cyclohexamide tracking.",{"name":119,"@type":110,"acceptedAnswer":120},"What effects does the UCHL3/EEF1A1 axis have on HCC cells and tumor progression?",{"text":121,"@type":113},"UCHL3 promotes HCC cell migration, stemness, and drug resistance; lowering EEF1A1 can reverse UCHL3-driven malignant behaviors, and nude mouse models support the axis in tumor progression.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},333510,1790738438,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":39,"category_name":40,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":34,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":139,"language":140,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":67,"update_tm":144,"read_time":145,"preview_page_count":4},4398048950312,"https://ap-avatar.wpscdn.com/avatar/400002538284de19e3c?_k=1778320343897328908","Zhao et al. Biology Direct (2024) 19:53 [https://doi.org/10.1186/s13062-024-00495-w](https://doi.org/10.1186/s13062-024-00495-w)  \nBiology Direct  \nRESEARCH Open Access  \nUCHL3 promotes hepatocellular carcinoma progression by stabilizing EEF1A1 through deubiquitination  \nJie Zhao 1,2, Qiang Huo3, Ji Zhang 1, Kexiang Sun 1, Jinhui Guo4, Feng Cheng 1*, Xiaoge Hu2* and Qiuran Xu2*  \nAbstract  \nBackground Hepatocellular carcinoma (HCC) ranks as the second leading cause of global cancer-related deaths and is characterized by a poor prognosis. Eukaryotic translation elongation factor 1 alpha 1 (EEF1A1) have been proved to play important roles in various human cancers, whereas the deubiquitination of EEF1A1 was poorly understood. Methods The binding and regulatory relationship between Ubiquitin carboxyl-terminal hydrolase L3 (UCHL3) and EEF1A1 was validated using clinical tissue samples, reverse transcription quantitative real-time fluorescence quantitative PCR (RT-qPCR), Western blotting, co-immunoprecipitation, and immunofluorescence, as well as ubiquitin detection and cyclohexamide tracking experiments. Finally, the impact of the UCHL3/EEF1A1 axis on HCC malignant behavior was analyzed through functional experiments and nude mouse models.  \nResults UCHL3 was found to have a high expression level in HCC tissues. Tissue samples from 60 HCC patients were used to evaluate the correlation between UCHL3 and EEF1A1 . UCHL3 binds to EEF1A1 through the lysine site, which reduces the ubiquitination level of EEF1A1 . Functional experiments and nude mouse models have demonstrated that the UCHL3/EEF1A1 axis promotes the migration, stemness, and drug resistance of HCC cells. Reducing the expression of EEF1A1 can reverse the effect of UCHL3 on the malignant behavior of HCC cells.  \nConclusion Our findings revealed that UCHL3 binds and stabilizes EEF1A1 through deubiquitination. UCHL3 and EEF1A1 formed a functional axis in facilitating the malignant progression of HCC, proving new insights for the antitumor targeted therapy for HCC.  \nKeywords Hepatocellular carcinoma, EEF1A1, UCHL3, Deubiquitination, Stemness  \n*Correspondence:  \nFeng Cheng [fengcheng@zjut.edu.cn](fengcheng@zjut.edu.cn)[ ](fengcheng@zjut.edu.cn)Xiaoge Hu [huxiaoge@hmc.edu.cn](huxiaoge@hmc.edu.cn)[ ](huxiaoge@hmc.edu.cn)Qiuran Xu [xuqiuran@hmc.edu.cn](xuqiuran@hmc.edu.cn)  \n1College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China  \n2Zhejiang Key Laboratory of Tumor Molecular Diagnosis and Individualized Medicine, Zhejiang Provincial People’s Hospital, Affiliated People’s Hospital, Zhejiang Provincial People’s Hospital, Hangzhou Medical College, Hangzhou, China  \n3Department of General Surgery, Zhoushan Dinghai Central Hospital (Dinghai District of Zhejiang Provincial People’s Hospital), Zhoushan, China  \n4Qingdao Medical College, Qingdao University, Qingdao, China  \n© The Author(s) 2024. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit [http://creativecommons.org/l](http://creativecommons.org/l)icenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ([http://creativecommons.org/publicdomain/zero/1.0/](http://creativecommons.org/publicdomain/zero/1.0/)) applies to the data made availab","cbCaiejAtzZlx09J","https://ap.wps.com/l/cbCaiejAtzZlx09J","pdf",11117511,11,"English","# Abstract\n## Background\n## Methods\n## Results\n## Conclusion\n# Introduction","[{\"question\":\"What biological mechanism does the paper propose between UCHL3 and EEF1A1 in HCC?\",\"answer\":\"The study proposes that UCHL3 binds to EEF1A1 at a lysine site, reduces EEF1A1 ubiquitination, and stabilizes EEF1A1 through deubiquitination.\"},{\"question\":\"How was the UCHL3–EEF1A1 relationship validated in this research?\",\"answer\":\"It was validated using clinical tissue samples and multiple molecular approaches including RT-qPCR, Western blotting, co-immunoprecipitation, immunofluorescence, ubiquitin detection, and cyclohexamide tracking.\"},{\"question\":\"What effects does the UCHL3/EEF1A1 axis have on HCC cells and tumor progression?\",\"answer\":\"UCHL3 promotes HCC cell migration, stemness, and drug resistance; lowering EEF1A1 can reverse UCHL3-driven malignant behaviors, and nude mouse models support the axis in tumor progression.\"}]","UCHL3 promotes hepatocellular carcinoma progression by stabilizing EEF1A1 through deubiquitination | PDF",1790002819,28]