Targeting ubiquitination for cancer therapies

Ubiquitination, the structured degradation and turnover of cellular proteins, is regulated by the ubiquitin-proteasome system (UPS). Most proteins that are critical for cellular regulations and functions are targets of the process. Ubiquitination is comprised of a sequence of three enzymatic steps,...

Full description

Saved in:
Bibliographic Details
Published in:Future medicinal chemistry 2015-11, Vol.7 (17), p.2333-2350
Main Authors: Morrow, John Kenneth, Lin, Hui-Kuan, Sun, Shao-Cong, Zhang, Shuxing
Format: Article
Language:English
Subjects:
Carrier Proteins - antagonists & inhibitors
Carrier Proteins - metabolism
Humans
Immunosuppressive Agents - chemistry
Immunosuppressive Agents - pharmacology
Immunosuppressive Agents - therapeutic use
Neoplasms - drug therapy
Neoplasms - metabolism
Neoplasms - pathology
Proteasome Inhibitors - chemistry
Proteasome Inhibitors - pharmacology
Proteasome Inhibitors - therapeutic use
Protein Interaction Domains and Motifs - drug effects
Review
Ubiquitin-Protein Ligases - antagonists & inhibitors
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
Ubiquitins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Ubiquitination, the structured degradation and turnover of cellular proteins, is regulated by the ubiquitin-proteasome system (UPS). Most proteins that are critical for cellular regulations and functions are targets of the process. Ubiquitination is comprised of a sequence of three enzymatic steps, and aberrations in the pathway can lead to tumor development and progression as observed in many cancer types. Recent evidence indicates that targeting the UPS is effective for certain cancer treatment, but many more potential targets might have been previously overlooked. In this review, we will discuss the current state of small molecules that target various elements of ubiquitination. Special attention will be given to novel inhibitors of E3 ubiquitin ligases, especially those in the SCF family.
ISSN:1756-8919
1756-8927
DOI:10.4155/fmc.15.148