USP34

USP34

USP34 stands for Ubiquitin Specific Peptidase 34. It is an enzyme that plays a crucial role in the regulation of protein degradation within cells. USP34 is a member of the deubiquitinating enzyme (DUB) family, which is responsible for removing ubiquitin molecules from proteins.

Function

USP34 is primarily involved in the removal of ubiquitin chains from target proteins, thereby preventing their degradation by the proteasome. By deubiquitinating proteins, USP34 helps to maintain protein homeostasis and regulate various cellular processes, including cell cycle progression, DNA repair, and signal transduction.

Structure

USP34 is a large protein consisting of multiple domains. It contains a catalytic domain, known as the ubiquitin-specific protease domain, which is responsible for its enzymatic activity. Additionally, USP34 possesses several other domains, such as the ubiquitin-associated (UBA) domain and the ubiquitin-like (UBL) domain, which are involved in protein-protein interactions and substrate recognition.

Role in Disease

Research has shown that USP34 dysregulation is associated with various diseases. For instance, aberrant expression or activity of USP34 has been observed in certain types of cancer, including breast cancer and colorectal cancer. In these cases, USP34 can promote tumor growth and metastasis by stabilizing oncogenic proteins or inhibiting the degradation of tumor suppressor proteins.

Furthermore, USP34 has been implicated in neurodegenerative disorders, such as Parkinson's disease and Alzheimer's disease. Dysfunctional USP34 can lead to the accumulation of misfolded proteins and the formation of toxic aggregates, contributing to the progression of these diseases.

References

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See Also

• Ubiquitin
• Proteasome
• Deubiquitinating enzyme
• Protein degradation
• Cell cycle
• DNA repair
• Signal transduction
• Breast cancer
• Colorectal cancer
• Parkinson's disease
• Alzheimer's disease