Constitutive photomorphogenic 1 E3 ubiquitin ligase (COP1)

Constitutive photomorphogenic 1 E3 ubiquitin ligase (COP1) is a RING-finger type E3 ubiquitin ligase conserved from plants to humans. COP1 mediates the transfer of ubiquitin to specific substrate proteins, marking them for degradation by the proteasome. In plants, COP1 acts as a central repressor of light-mediated development and operates in concert with SPA proteins and as part of a CUL4-DDB1-RBX1 ligase complex[1]. In mammals (also annotated as RFWD2), COP1 regulates the stability of key transcription factors and tumor suppressors, such as p53 and c-Jun, thereby modulating cell cycle progression, apoptosis, and oncogenic signaling. While its central roles in cellular homeostasis and cancer highlight COP1 as a potential therapeutic intervention point, there are currently no approved drugs specifically targeting COP1. Pharmacological modulation of E3 ligases like COP1 remains a promising but challenging area for drug development due to concerns about specificity and broad biological effects[1][2][3].

Other names

Constitutive photomorphogenic 1COP1RFWD2 (in humans)RING finger and WD repeat domain 2

Protein ubiquitination and proteasomal degradation (e.g., destabilization of p53 and c-Jun); Substrate-specific degradation in multi-protein E3 complexes