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This review summarizes DUB biology, emphasizing their roles in T-cell development, apoptosis, and oral cancers, and highlights their therapeutic potential as cancer targets.",{"@graph":14,"@context":73},[15,34,56],{"@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/healthcare/","Healthcare",3,{"item":32,"name":10,"@type":21,"position":33},"https://docshare.wps.com/document/deubiquitinases-and-cancer-review-article/369267/",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/deubiquitinases-and-cancer-review-article/369267.png","ImageObject",300,407,{"name":42,"@type":43},"Levi","Person",{"url":19,"name":45,"@type":46},"DocShare","Organization","application/pdf","2026-10-27","2026-09-23",true,{"@type":52,"interactionType":53,"userInteractionCount":55},"InteractionCounter",{"@type":54},"ViewAction",10,{"@type":57,"mainEntity":58},"FAQPage",[59,65,69],{"name":60,"@type":61,"acceptedAnswer":62},"What are deubiquitinases (DUBs) and what do they do in cells?","Question",{"text":63,"@type":64},"Deubiquitinases remove ubiquitin from ubiquitylated substrates, regulating protein activity and stability. They also process ubiquitin signals by trimming chains, generating free ubiquitin, and reversing ubiquitin signaling on targets.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"How are DUBs connected to cancer development?",{"text":68,"@type":64},"Dysregulation of DUBs contributes to carcinogenesis and cancer progression. DUBs affect key cancer-related processes such as proliferation, cell-cycle control, apoptosis, DNA damage response, tumor suppression, oncogenesis, and metastasis.",{"name":70,"@type":61,"acceptedAnswer":71},"Why is the review particularly focused on oral cancers and T-cell development?",{"text":72,"@type":64},"The review provides basic DUB knowledge and emphasizes their importance in T-cell development and apoptosis with a specific emphasis on oral cancers. 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They are involved in various cellular functions including proteasome‑ and lysosome‑dependent proteolysis, gene expression, cell cycle progression, chromosome segregation, kinase activation, histone modification, cell cycle regulation, cell differentiation, spermatogenesis, apoptosis, endocytosis, autophagy, localization, and DNA damage repair. On the other hand, it is also involved in the processes of carcinogenesis and cancer development. DUBs are related to different aspects of human cancer, including proliferation, cell cycle control, apoptosis, DNA damage response (DDR), tumor suppression, oncogenesis, and metastasis. Multiple processes involved in innate and adaptive immunity, such as antigen presentation, cell differentiation, immune defense, and inflammatory responses, are regulated by ubiquitination/deubiquitination. Dysregulation of DUBs is implicated in several human diseases, highlighting the importance of DUB function. This review also provides basic knowledge of DUBs in the development of cancersand highlights the importance of DUBs in T‑cell development, apoptosis, and cancer with a specific emphasis on oral cancers. This review highlights the recent advances in the field of cancer biology with a specific role in DUBs in cellular functions. The aberrant expression and regulation of these enzymes have been shown to contribute to promote tumorigenesis, making them promising therapeutic targets for cancer therapy.  \nKeywords: Apoptosis, cancer‑related pathway, DUB’s   \nIntroduction  \nost‑translational modifications (PTMs) of proteins  \nbycelsleveral proteincycle regulatiitinbygtheneirzymesenzymareatic afssociateunctionds The timed regulation and response to the proliferation and apoptosis signals of various proteins is a vital aspect of the mammalian cell cycle. One of the most pervasive PTMs is ubiquitination and deubiquitination which affects intracellular localization, stability, and function of target proteins.  \nUbiquitination is a three‑step enzymatic cascade involving E1, E2, and E3 enzymes that results in the transfer of ubiquitin, via its C‑terminal glycine, onto the ε‑amino group of a lysine residue on the substrate[1][Figure 1] . Several ubiquitination sites on thousands of proteins have been identified, indicating that most  \n\n| Access this article online |  |\n| --- | --- |\n| Quick Response Code:\u003Cbr>| Website: [https://journals.lww.com/jpbs](https://journals.lww.com/jpbs) |\n|  | DOI: 10.4103/jpbs.jpbs_517_24 |\n\ncellular proteins will experience ubiquitination at some point in their lifetime.  \nDeubiquitinating enzymes (DUBs) are proteases that play several roles in the ubiquitin pathway as they cleave ubiquitin or ubiquitin‑like proteins from proproteins or target proteins.[2] They have a reversible function for ubiquitination and are also important determinants of protein fate cell cycle processing. DUBs have three major cellular functions: (i) the generation of free Ub moieties from linear fusions of Ub[3,4]; (ii) trimming of existing polyubiquitin chains; and (iii) reversal of Ub signaling by removal of Ub chains from target  \nAddress for correspondence: Dr. Preethi Murali, Department of Oral and Maxillofacial Pathology and Oral Microbiology, Meenakshi Ammal Dental College and Hospital, MAHER, Chennai, Tamil Nadu, India.  \nE‑mail: [drpreethi.oralpathology@madch.edu.in](drpreethi.oralpathology@","cbCaic5fSdID0FyC","https://ap.wps.com/l/cbCaic5fSdID0FyC","pdf",952127,11,"English","# Abstract\n# Introduction\n## Post-translational modifications and ubiquitin signaling\n## Ubiquitination cascade and DUB functions\n# Classes of DUBs\n## Cysteine/metalloprotease DUB families\n## Other ubiquitin-like protease classes","[{\"question\":\"What are deubiquitinases (DUBs) and what do they do in cells?\",\"answer\":\"Deubiquitinases remove ubiquitin from ubiquitylated substrates, regulating protein activity and stability. They also process ubiquitin signals by trimming chains, generating free ubiquitin, and reversing ubiquitin signaling on targets.\"},{\"question\":\"How are DUBs connected to cancer development?\",\"answer\":\"Dysregulation of DUBs contributes to carcinogenesis and cancer progression. DUBs affect key cancer-related processes such as proliferation, cell-cycle control, apoptosis, DNA damage response, tumor suppression, oncogenesis, and metastasis.\"},{\"question\":\"Why is the review particularly focused on oral cancers and T-cell development?\",\"answer\":\"The review provides basic DUB knowledge and emphasizes their importance in T-cell development and apoptosis with a specific emphasis on oral cancers. It frames these roles as part of the broader involvement of DUBs in cancer biology.\"}]","Deubiquitinases and Cancer - review article | PDF",1790181661,28]