Ubiquitin ligases in cancer: Functions and clinical potentials

Ubiquitylation, a highly regulated post-translational modification, controls many cellular pathways that are critical to cell homeostasis. Ubiquitin ligases recruit substrates and promote ubiquitin transfer onto targets, inducing proteasomal degradation or non-degradative signaling. Accumulating evidence highlights the critical role of dysregulated ubiquitin ligases in processes associated with the initiation and progression of cancer. Depending on the substrate specificity and biological context, a ubiquitin ligase can act either as a tumor promoter or as a tumor suppressor. In this review, we focus on the regulatory roles of ubiquitin ligases and how perturbations of their functions contribute to cancer pathogenesis. We also briefly discuss current strategies for targeting or exploiting ubiquitin ligases for cancer therapy.

Automated summary

Ubiquitylation is a crucial post-translational modification that regulates many cellular pathways. Dysregulated ubiquitin ligases play critical roles in cancer initiation and progression, acting as either tumor promoters or tumor suppressors depending on substrates and contexts. Current research focuses on understanding the regulatory roles of ubiquitin ligases and developing strategies for cancer therapy.