CHFR Protein, Human

CHFR, an E3 ubiquitin-protein ligase, plays a crucial role in the antephase checkpoint, actively impeding the entry into mitosis in response to microtubule poisons. Its action commences in early prophase, preceding chromosome condensation, particularly when the centrosomes relocate along the nuclear periphery. CHFR is implicated in signaling the presence of mitotic stress induced by microtubule poisons, accomplishing this by catalyzing 'Lys-48'-linked ubiquitination of target proteins, leading to their subsequent degradation through the proteasome. Notably, CHFR orchestrates the ubiquitination and degradation of key mitotic regulators such as AURKA and PLK1. This multifaceted protein is likely to function as a tumor suppressor, potentially mediating the polyubiquitination of HDAC1, thereby targeting it for degradation. Moreover, CHFR may facilitate the formation of 'Lys-63'-linked polyubiquitin chains, collaborating with the UBC13-MMS2 heterodimer, where substrates marked with 'Lys-63' polyubiquitin chains typically participate in signaling cellular stress rather than facing degradation.