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Ubiquitin carboxyl-terminal hydrolase 14 (USP14)
- Target
- USP14
- Molecular classification
- Enzyme, Deubiquitinating enzyme (DUB), Peptidase C19 family, USP14/UBP6 subfamily
01
Overview
Ubiquitin carboxyl-terminal hydrolase 14 (USP14) is a deubiquitinating enzyme that removes ubiquitin from polyubiquitinated proteins, primarily those targeted for degradation by the proteasome. It is involved in various cellular processes, including protein quality control, immune response, and regulation of synaptic function. USP14 exists in an autoinhibited state and is activated upon binding to the proteasome. Its dysregulation is implicated in several diseases, including cancer and neurodegenerative disorders, making it a potential therapeutic target. Small molecule inhibitors are being investigated as research tools.
02
Mechanism of action
Inhibition of USP14's deubiquitinating activity.
03
Biological functions
Protein deubiquitinationRegulation of chemotaxisSynaptic transmissionNeuromuscular junction development/functionUbiquitin-dependent protein catabolic processEndoplasmic reticulum-associated degradation (ERAD)Regulation of proteasomal activityRegulation of autophagyImmune responseViral infections
04
Disease associations
Cancer progressionNeurodegenerative diseasesDefects in immune responsePathologies related to impaired protein homeostasis
05
Safety considerations
Off-target effects when inhibiting USP14.
06
Interacting drugs
IU1
1 more in the full profile.
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