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Significance Ubiquitination of several DNA replication–repair proteins is a critical mechanism by which cellular DNA replication and DNA damage repair pathways are controlled. The E3 ligase RING finger and WD repeat domain-containing protein 3 (RFWD3) has emerged as an important regulator of genome stability. We propose that the association of RFWD3 to proliferating cell nuclear antigen stabilizes RFWD3 at the fork, enabling ubiquitination of replication protein A and its subsequent removal to facilitate DNA replication.

PCNA-mediated stabilization of E3 ligase RFWD3 at the replication fork is essential for DNA replication