RBR E3 ubiquitin ligases in tumorigenesis.

Carrier Proteins / metabolism Female Humans Neoplasms / genetics Transferases / metabolism Ubiquitin-Protein Ligases / chemistry
Degradation Oncogene RBR E3 Tumor suppressor Ubiquitination

Journal

Seminars in cancer biology
ISSN: 1096-3650
Titre abrégé: Semin Cancer Biol
Pays: England
ID NLM: 9010218

Informations de publication

Date de publication:
Dec 2020
Historique:
received: 06 04 2020
revised: 28 04 2020
accepted: 04 05 2020
pubmed: 23 5 2020
medline: 16 9 2021
entrez: 23 5 2020
Statut: ppublish

Résumé

RING-in-between-RING (RBR) E3 ligases are one class of E3 ligases that is characterized by the unique RING-HECT hybrid mechanism to function with E2s to transfer ubiquitin to target proteins for degradation. Emerging evidence has demonstrated that RBR E3 ligases play essential roles in neurodegenerative diseases, infection, inflammation and cancer. Accumulated evidence has revealed that RBR E3 ligases exert their biological functions in various types of cancers by modulating the degradation of tumor promoters or suppressors. Hence, we summarize the differential functions of RBR E3 ligases in a variety of human cancers. In general, ARIH1, RNF14, RNF31, RNF144B, RNF216, and RBCK1 exhibit primarily oncogenic roles, whereas ARIH2, PARC and PARK2 mainly have tumor suppressive functions. Moreover, the underlying mechanisms by which different RBR E3 ligases are involved in tumorigenesis and progression are also described. We discuss the further investigation is required to comprehensively understand the critical role of RBR E3 ligases in carcinogenesis. We hope our review can stimulate the researchers to deeper explore the mechanism of RBR E3 ligases-mediated carcinogenesis and to develop useful inhibitors of these oncogenic E3 ligases for cancer therapy.

Identifiants

DOI: 10.1016/j.semcancer.2020.05.002 PMID: 32442483
pubmed: 32442483
pii: S1044-579X(20)30098-5
doi: 10.1016/j.semcancer.2020.05.002
pii:
doi:

Substances chimiques

Carrier Proteins 0
Cul9 protein, human EC 2.-
Transferases EC 2.-
ARIH1 protein, human EC 2.3.2.27
ARIH2 protein, human EC 2.3.2.27
RNF144A protein, human EC 2.3.2.27
RNF144B protein, human EC 2.3.2.27
RNF216 protein, human EC 2.3.2.27
RNF31 protein, human EC 2.3.2.27
Ubiquitin-Protein Ligases EC 2.3.2.27

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

131-144

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Auteurs

Peter Wang (P)

School of Laboratory Medicine, Bengbu Medical College, Anhui, 233030, China.

Xiaoming Dai (X)

Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Ave., Boston, MA, USA.

Wenxiao Jiang (W)

Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou 325027, Zhejiang, China.

Yuyun Li (Y)

School of Laboratory Medicine, Bengbu Medical College, Anhui, 233030, China. Electronic address: bbmcliyuyun@163.com.

Wenyi Wei (W)

Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Ave., Boston, MA, USA. Electronic address: wwei2@bidmc.harvard.edu.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female

Evaluation of Low-Value Services Across Major Medicare Advantage Insurers and Traditional Medicare.

Ciara Duggan, Adam L Beckman, Ishani Ganguli et al.
1.00
Humans United States Aged Cross-Sectional Studies Medicare Part C

Effectiveness of Virtual Yoga for Chronic Low Back Pain: A Randomized Clinical Trial.

Hallie Tankha, Devyn Gaskins, Amanda Shallcross et al.
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › RBR E3 ubiquitin ligases in tumorigenesis.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › RBR E3 ubiquitin ligases in tumorigenesis.
questionsmedicales.fr › Tumeurs › RBR E3 ubiquitin ligases in tumorigenesis.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › RBR E3 ubiquitin ligases in tumorigenesis.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › RBR E3 ubiquitin ligases in tumorigenesis.