Deubiquitinase Assay Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

De-ubiquitinating enzymes (DUBs) function mechanically by removing ubiquitin moieties from proteins reversing what ubiquitination does. This action regulates protein degradation localization and activity. DUBs include enzymes such as ubiquitin-specific proteases (USPs) and ubiquitin C-terminal hydrolases (UCHs). These enzymes are typically expressed in various tissues throughout the body aligning with their roles in multiple cellular processes. DUB molecular masses vary widely reflecting the diverse structures and functions within this enzyme family.

Biological function summary

De-ubiquitination regulates protein stability and function impacting processes like DNA repair cell cycle and signal transduction. DUBs may operate as part of a larger complex interfacing with other protein groups to maintain cellular equilibrium. They handle ubiquitin chains after proteins have been tagged for degradation critical for maintaining cellular proteostasis.

Pathways

De-ubiquitinating enzymes integrate into systems that oversee protein quality control and signal transduction. Key pathways include the ubiquitin-proteasome system and the endoplasmic reticulum-associated degradation (ERAD) pathway. Related proteins within these pathways include E3 ligases such as Mdm2 and substrate proteins like p53 as de-ubiquitination dictates their fates and manipulation in cellular environments.

Associated diseases and disorders

De-ubiquitinating enzymes have roles in cancer and neurodegenerative diseases. Alterations in DUB activities link to disorders such as Parkinson's disease and various cancers through their role in protein regulation and signal pathways. For instance DUBs influence the stability of proteins like p53 in cancer and alpha-synuclein in Parkinson's disease pointing to their importance in disease progression and therapeutic targeting.