Abstract
Ubiquitination represents a post-translational modification (PTM) essential for the maintenance of cellular homeostasis. Ubiquitination is involved in the regulation of protein function, localization and turnover through the attachment of a ubiquitin molecule(s) to a target protein. Ubiquitination can be reversed through the action of deubiquitinating enzymes (DUBs). The DUB enzymes have the ability to remove the mono- or poly-ubiquitination signals and are involved in the maturation, recycling, editing and rearrangement of ubiquitin(s). Ubiquitin-specific proteases (USPs) are the biggest family of DUBs, responsible for numerous cellular functions through interactions with different cellular targets. Over the past few years, several studies have focused on the role of USPs in carcinogenesis, which has led to an increasing development of therapies based on USP inhibitors. In this review, we intend to describe different cellular functions, such as the cell cycle, DNA damage repair, chromatin remodeling and several signaling pathways, in which USPs are involved in the development or progression of cancer. In addition, we describe existing therapies that target the inhibition of USPs.
Highlights
Cancer is an important health problem, representing the second most deathly pathology in the world
The establishment of the isopeptide bond, HIF1α suffers conformational changes between the C-terminal carboxyl group of a ubiquitin and the amino group of a lysine and migrates to the nucleus, where it interacts with HIF1α and is responsible for the of a target protein is accomplished by the participation of three families of enzymes: E1 transcription of several genes that favor tumoral growth
The mechanisms are not completely established, it seems that USP39 knockdown induced an increase in E-cadherin levels through the Wnt/β-catenin signaling pathway, avoiding cellular migration [79,149]
Summary
Cancer is an important health problem, representing the second most deathly pathology in the world. The establishment of the isopeptide bond (similar to what happen in hypoxia conditions), HIF1α suffers conformational changes between the C-terminal carboxyl group of a ubiquitin and the amino group of a lysine and migrates to the nucleus, where it interacts with HIF1α and is responsible for the of a target protein is accomplished by the participation of three families of enzymes: E1 transcription of several genes that favor tumoral growth. In situations of loss of VHL function (similar to what happen in hypoxia conditions), HIF1α suffers conformational changes and migrates to the nucleus, where it interacts with HIF1α and is responsible for the transcription of several genes that favor tumoral growth One of these genes is vascular endothelial growth factor (VEGF), involved in angiogenesis, leading to an increase in the vascularization, promoting a rise in oxygen levels and potentiate tumoral growth. One of these genes is vascular endothelial growth factor (VEGF), involved in angiogenesis, leading to an increase in the vascularization, promoting a rise in oxygen levels and potentiate tumoral growth. [34]
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