[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-seo-350032-105":3,"detail-sidebar-cat-0-en-105":80,"doc-detail-350032-en":130},{"code":4,"msg":5,"data":6},0,"ok",{"site_id":7,"language":8,"slug":9,"title":10,"keywords":11,"description":12,"schema_data":13,"social_meta":73,"head_meta":75,"extra_data":77,"updated_unix":79},105,"en","dual-roles-of-ubiquitin-specific-peptidase-10-usp10-in-cancer-review","Dual Roles of Ubiquitin-Specific Peptidase 10 (USP10) in Cancer - Review","","Ubiquitin-specific peptidase 10 (USP10) deubiquitinates multiple signaling proteins in cancer cells. Because its substrates can include both tumor suppressors and oncogenic proteins, USP10 can exert inhibitory as well as promoting effects on tumorigenesis and disease progression. This review summarizes the dual roles of USP10 across diverse cancer types, including hepatocellular carcinoma, lung cancer, breast cancer, prostate cancer, gastric cancer, and acute and chronic myelogenous leukemia. It also discusses how USP10 dysregulation relates to cancer development and the therapeutic potential of USP10 inhibitors as targeted anticancer drugs.",{"@graph":14,"@context":72},[15,34,55],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/research-report/","Research & Report",3,{"item":32,"name":10,"@type":21,"position":33},"https://docshare.wps.com/document/dual-roles-of-ubiquitin-specific-peptidase-10-usp10-in-cancer-review/350032/",4,{"url":32,"name":10,"@type":35,"image":36,"author":41,"headline":10,"publisher":44,"fileFormat":47,"inLanguage":8,"description":12,"dateModified":48,"datePublished":49,"encodingFormat":47,"isAccessibleForFree":50,"interactionStatistic":51},"DigitalDocument",{"url":37,"@type":38,"width":39,"height":40},"https://docshare.wps.com/thumbnails/dual-roles-of-ubiquitin-specific-peptidase-10-usp10-in-cancer-review/350032.png","ImageObject",300,407,{"name":42,"@type":43},"Jacob","Person",{"url":19,"name":45,"@type":46},"DocShare","Organization","application/pdf","2026-09-23","2026-09-22",true,{"@type":52,"interactionType":53,"userInteractionCount":26},"InteractionCounter",{"@type":54},"ViewAction",{"@type":56,"mainEntity":57},"FAQPage",[58,64,68],{"name":59,"@type":60,"acceptedAnswer":61},"What is USP10’s core function in cancer cells?","Question",{"text":62,"@type":63},"USP10 removes ubiquitin chains from target signaling proteins through deubiquitination. This alters protein stability and activity in cancer-related pathways.","Answer",{"name":65,"@type":60,"acceptedAnswer":66},"Why does USP10 show both inhibitory and promoting effects on tumors?",{"text":67,"@type":63},"USP10 substrates can include both tumor suppressors and oncogenic proteins. As a result, deubiquitination can either prevent or enhance tumorigenesis and progression depending on the substrate context.",{"name":69,"@type":60,"acceptedAnswer":70},"Which cancer types are discussed regarding USP10’s dysregulation?",{"text":71,"@type":63},"The review covers hepatocellular carcinoma, lung cancer, breast cancer, prostate cancer, gastric cancer, and acute and chronic myelogenous leukemia, focusing on associations between aberrant USP10 expression and development of these cancers.","https://schema.org",{"og:url":32,"og:type":74,"og:title":10,"og:site_name":45,"og:description":12},"article",{"robots":76,"canonical":32},"index,follow",{"doc_id":78,"site_id":7},350032,1790195678,{"code":4,"msg":81,"data":82},"success",[83,87,91,95,100,105,110,114,119,122,126],{"id":22,"doc_module":4,"doc_module_name":25,"category_name":84,"show_sort_weight":85,"slug":86},"Story & Novel",90,"story-novel",{"id":26,"doc_module":4,"doc_module_name":25,"category_name":88,"show_sort_weight":89,"slug":90},"Literature",80,"literature",{"id":33,"doc_module":4,"doc_module_name":25,"category_name":92,"show_sort_weight":93,"slug":94},"Exam",70,"exam",{"id":96,"doc_module":4,"doc_module_name":25,"category_name":97,"show_sort_weight":98,"slug":99},5,"Comic",60,"comic",{"id":101,"doc_module":4,"doc_module_name":25,"category_name":102,"show_sort_weight":103,"slug":104},6,"Technology",50,"technology",{"id":106,"doc_module":4,"doc_module_name":25,"category_name":107,"show_sort_weight":108,"slug":109},7,"Healthcare",40,"healthcare",{"id":111,"doc_module":4,"doc_module_name":25,"category_name":29,"show_sort_weight":112,"slug":113},8,30,"research-report",{"id":115,"doc_module":4,"doc_module_name":25,"category_name":116,"show_sort_weight":117,"slug":118},9,"Religion & Spirituality",20,"religion-spirituality",{"id":117,"doc_module":4,"doc_module_name":25,"category_name":120,"show_sort_weight":117,"slug":121},"World Cup","world-cup",{"id":123,"doc_module":4,"doc_module_name":25,"category_name":124,"show_sort_weight":123,"slug":125},10,"Lifestyle","lifestyle",{"id":127,"doc_module":4,"doc_module_name":25,"category_name":128,"show_sort_weight":96,"slug":129},19,"General","general",{"code":4,"msg":81,"data":131},{"doc_id":78,"user_id":132,"nickname":42,"user_avatar":133,"doc_module":4,"category_id":111,"category_name":29,"doc_title":10,"doc_description":12,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":26,"is_deleted":4,"is_public":22,"is_downloadable":22,"audit_status":22,"page_count":139,"language":140,"language_code":8,"site_id":7,"html_lang":8,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":12,"update_tm":144,"read_time":145},962084931830,"https://ap-avatar.wpscdn.com/davatar_a8503ba1806abce46bf441b54a3ca4cd","Review  \nDual Roles of Ubiquitin-Specific Peptidase 10 (USP10) in Cancer  \nYifei Zhai, Liming Zhou, Manhan Zhao and Qiong Lin *  \nAcademic Editor: Hengbin Wang  \nReceived: 11 February 2026  \nRevised: 5 March 2026  \nAccepted: 8 March 2026  \nPublished: 13 March 2026  \nCopyright: © 2026 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.  \nSchool of Medicine, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China;  \n[2212413005@stmail.ujs.edu.cn](2212413005@stmail.ujs.edu.cn) (Y.Z.); [2212313098@stmail.ujs.edu.cn](2212313098@stmail.ujs.edu.cn) (L.Z.); [2212313096@stmail.ujs.edu.cn](2212313096@stmail.ujs.edu.cn) (M.Z.)  \n* Correspondence: [qlin@ujs.edu.cn](qlin@ujs.edu.cn)  \nAbstract  \nUbiquitin-specific peptidase 10 (USP10) deubiquitinates multiple signaling proteins in cancer cells. These USP10 substrates contain both tumor suppressors and oncogenic proteins, thus conferring both inhibitory and promoting effects of USP10 on tumorigenesis and progression. This review focuses on the dual roles of USP10 in various cancer types and addresses the association of aberrant USP10 expression with the development of various types of cancers, including hepatocellular carcinoma, lung cancer, breast cancer, prostate cancer, gastric cancer, and acute and chronic myelogenous leukemia. In addition, this review discusses the potential applications of USP10 inhibitors as targeted drugs for cancer therapy.  \nKeywords: USP10; deubiquitination; cancers; USP10 inhibitors; cancer therapy  \n1. Overview of Deubiquitinating Enzymes (DUBs) and Ubiquitin-Specific Peptidases (USPs)  \nDeubiquitination is a reversible biochemical process of removing ubiquitin chains from ubiquitinated proteins that is catalyzed by DUBs. Deubiquitination plays a pivotal role in maintaining cellular homeostasis by regulating protein stability, interaction, activity, and subcellular localization [1–3] . DUBs function in multiple cellular processes, including gene expression, DNA repair, cell cycle, and apoptosis [4] .  \nThere are more than 100 DUBs found in human cells. DUBs are categorized into seven groups based on their sequence and structural domains, including ubiquitin-specific peptidases (USPs), ubiquitin carboxy-terminal hydrolases (UCHs), ovarian tumor proteases (OTUs), Machado–Joseph disease proteases (MJDs), novel miu-containing DUB family (MINDY) proteases, Jab1/MPN/MOV34 metalloenzymes (JAMMs), and Znfinger and UFSP structural domain proteins (ZUFSPs) [5–7] .  \nThe USP family is the largest DUB group, with more than 50 members. The USP members have a conserved USP domain comprising three regions: the deubiquitination catalytic region, the ubiquitin-binding region, and the substrate-binding region. These three regions of the USP domain are analogized to the finger, thumb, and palm, and have cysteine protease activity [8,9] . The USP catalytic region contains cysteine, histidine, and aspartate or glutamate residues that are responsible for hydrolyzing the ubiquitin chain [10] . Members of the USP family have variable sizes of USP domains that range from 300 to 800 amino acids [4] . USP members interact with the ubiquitin chain via blocking loops or specific ubiquitin-binding hotspots, combined with other protein-interactive domains, to determine substrate specificity [11] . Previous studies have shown that the auxiliary domains of USPs, such as ubiquitin-associated domains (UBA), ubiquitin-interaction motifs  \n(UIM), and zinc-finger ubiquitin-specific protease domains (ZnF-UBP), enhance binding to ubiquitinated substrates [12] .  \nUSP family members play dual roles in cancers by inhibiting the degradation of either tumor suppressors or oncogenic proteins [13] . In addition, USP family members promote immune evasion by interfering with antigen processing and presentation [14] .  \nIn this review, we will address the dual roles of USP1","cbCaibnWkhdYAavW","https://ap.wps.com/l/cbCaibnWkhdYAavW","pdf",1460142,26,"English","# Abstract\n# Overview of Deubiquitinating Enzymes (DUBs) and Ubiquitin-Specific Peptidases (USPs)\n## Classification and roles of DUBs\n## USP family structure and catalytic features\n## USP family involvement in cancer biology\n# USP10 and Its Cellular Function\n## Deubiquitinase-dependent cellular functions of USP10","[{\"question\":\"What is USP10’s core function in cancer cells?\",\"answer\":\"USP10 removes ubiquitin chains from target signaling proteins through deubiquitination. This alters protein stability and activity in cancer-related pathways.\"},{\"question\":\"Why does USP10 show both inhibitory and promoting effects on tumors?\",\"answer\":\"USP10 substrates can include both tumor suppressors and oncogenic proteins. As a result, deubiquitination can either prevent or enhance tumorigenesis and progression depending on the substrate context.\"},{\"question\":\"Which cancer types are discussed regarding USP10’s dysregulation?\",\"answer\":\"The review covers hepatocellular carcinoma, lung cancer, breast cancer, prostate cancer, gastric cancer, and acute and chronic myelogenous leukemia, focusing on associations between aberrant USP10 expression and development of these cancers.\"}]","Dual Roles of Ubiquitin-Specific Peptidase 10 (USP10) in Cancer - Review | PDF",1790086840,66]