PARC (gene)

PARC, also known as CUL9, is a human gene encoding a protein involved in the regulation of cell cycle progression, DNA damage response, and protein ubiquitination. It is part of the cullin-RING ubiquitin ligase (CRL) family, specifically acting as a scaffold protein within the CRL9 complex. The CRL9 complex is an E3 ubiquitin ligase that targets specific proteins for degradation via the ubiquitin-proteasome pathway.

The PARC protein interacts with other proteins, including Rbx1 (also known as Roc1), DDB1, and DCUN1D1. These interactions are essential for the formation and function of the CRL9 complex. The specific targets of the CRL9 complex, and thus the precise cellular processes influenced by PARC, are still being actively researched, but evidence suggests a role in regulating DNA replication, DNA repair, and the stability of certain oncoproteins.

Dysregulation of PARC expression or function has been implicated in various cancers. Aberrant expression levels have been observed in certain tumor types, suggesting that PARC may play a role in tumorigenesis and cancer progression. Studies have explored PARC as a potential therapeutic target, focusing on modulating its activity to influence the cellular processes it regulates.

Further research is ongoing to fully elucidate the precise mechanisms and cellular roles of PARC, as well as its significance in various diseases.