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This review summarizes how dysregulated RBBP6 expression and function drive cancer development and therapeutic response through interactions with E3 ligase substrates, JNK signaling, noncoding RNAs, and DNA damage-associated proteins. 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Ubanako  \n [ubanakophil@gmail.com](ubanakophil@gmail.com)[ ](ubanakophil@gmail.com)Clement Penny  \n [clement.penny@wits.ac.za](clement.penny@wits.ac.za)[ ](clement.penny@wits.ac.za)RECEIVED 29 March 2026 REVISED 24 April 2026 ACCEPTED 30 April 2026 PUBLISHED 19 May 2026  \nCITATION  \nUbanako PN, Nweke EE, Nsingwane Z, Monchusi B and Penny C (2026) RBBP6 and cancer: from molecular mechanisms to clinical implications.  \nFront. Oncol. 16:1841906 .  \ndoi: 10.3389/fonc.2026.1841906  \nCOPYRIGHT  \n© 2026 Ubanako, Nweke, Nsingwane, Monchusi and Penny. This is an openaccess article distributed under the terms of the Creative Commons Attribution License (CC BY) . The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.  \nRBBP6 and cancer: from molecular mechanisms to clinical implications  \nPhilemon N. Ubanako 1*, Ekene E. Nweke 2,3, Zanele Nsingwane 4, Bernice Monchusi 1,5 and Clement Penny 1*  \n1 Molecular and Cellular Oncology Research Group, Department of Internal Medicine, Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, South Africa, 2 Department of Surgery, Faculty of Health Sciences, University of the Witwatersrand, Johannesburg, South Africa, 3 Department of Life and Consumer Sciences, University of South Africa, Johannesburg, South Africa, 4Wits Diagnostic and Innovation Hub, Wits Health Consortium, University of the Witwatersrand, Johannesburg, South Africa, 5 Department of Biosciences, Council for Scientific and Industrial Research (CSIR), Pretoria, South Africa  \nRetinoblastoma binding protein 6 (RBBP6) is a 200 kDa E3 ubiquitin ligase that performs several biological functions and plays a role in tumorigenesis. RBBP6 is overexpressed in several types of tumors, including lung, colorectal, breast, cervical, hepatocellular, and esophageal cancers, suggesting its association with malignant progression. Moreover, this increased expression has been associated with clinicopathological parameters in lung, colorectal, cervical, and ovarian cancers. This review captures the molecular functions of RBBP6 and the mechanisms by which aberrant RBBP6 expression and function influence cancer development and therapeutic response. These mechanisms include its ability to interact with E3 ligase substrates, Jun N-terminal kinase (JNK), noncoding RNAs, and DNA damage-associated proteins to promote cell proliferation, stemness, cell cycle progression, and metastasis. We also evaluated the prognostic and predictive significance of RBBP6 as a potential cancer biomarker and its suitability as a molecular target in cancer. This is the first review that comprehensively explores the multifaceted molecular mechanisms by which RBBP6 influences cancer progression in several cancer types.  \nKEYWORDS  \nbiomarker, cancer, carcinogenesis, gene regulation, molecular mechanisms, posttranslational modifications, RBBP6, ubiquitin ligase  \n1 Introduction  \nRetinoblastoma binding protein 6 (RBBP6) is a 200 kDa mRNA splicing-associated protein with E3 ubiquitin ligase activity conferred by a RING finger domain (1) . RBBP6 functions include ubiquitination, mRNA processing, cell cycle control, apoptosis, and DNA replication (2–5) . Loss of RBBP6 leads to early embryonic lethality in mice, emphasizing its critical role in cell viability and development. RBBP6 interacts with two key tumor suppressor proteins, p53 and retinobl","cbCaiicQ2jAZ6V3J","https://ap.wps.com/l/cbCaiicQ2jAZ6V3J","pdf",1003867,16,"English","# Introduction\n# RBBP6 protein structure and isoforms","[{\"question\":\"What is RBBP6, and why is it important in cancer?\",\"answer\":\"RBBP6 is a 200 kDa E3 ubiquitin ligase involved in multiple biological functions. Its overexpression in several tumors is associated with malignant progression and clinical parameters.\"},{\"question\":\"Through which mechanisms does RBBP6 promote tumor development?\",\"answer\":\"The review describes RBBP6 interactions with E3 ligase substrates, JNK signaling, noncoding RNAs, and DNA damage-associated proteins, which can promote proliferation, stemness, cell-cycle progression, and metastasis.\"},{\"question\":\"How is RBBP6 evaluated as a biomarker or therapeutic target?\",\"answer\":\"The review assesses the prognostic and predictive significance of RBBP6 and discusses its suitability as a molecular target in cancer therapy.\"}]","RBBP6 and cancer - from molecular mechanisms to clinical implications - Review | PDF",1790109738]