Regulatory role of E3 ubiquitin ligases in multiple myeloma: from molecular mechanisms to therapeutic strategies

TL;DR

This review explores how E3 ubiquitin ligases influence multiple myeloma and their potential as therapeutic targets.

Contribution

The paper provides a comprehensive overview of the emerging roles of E3 ubiquitin ligases in multiple myeloma therapy.

Findings

E3 ubiquitin ligases regulate protein ubiquitination, affecting protein degradation and signaling in MM.

They contribute to MM progression and drug resistance, making them potential therapeutic targets.

Understanding their mechanisms could lead to improved treatment strategies for MM patients.

Abstract

Multiple myeloma (MM) is a hematological tumor characterized by the malignant proliferation of plasma cells in bone marrow (BM). Despite the prolonged survival of MM patients, a significant amount of patients relapse or become drug resistant. This underlines the importance of the development and investigation of novel targets to improve MM therapy. Increasing evidences have shed light on the emerging roles of E3 ubiquitin ligases in MM. E3 ubiquitin ligases play an essential role in protein ubiquitination, which is involved in the regulation of protein degradation, protein-protein interactions and signal transduction. In this comprehensive review, we will summarize the current understanding of E3 ubiquitin ligases in MM and their contribution to MM therapy, which could help explore the molecular mechanisms in MM and provide potential therapeutic targets for the treatment of MM.

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