{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lin YC"],"funding":["HHS | NIH | National Institute of General Medical Sciences","NCI NIH HHS","NIGMS NIH HHS","National Science Foundation"],"pagination":["13282-13287"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6310862"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["115(52)"],"pubmed_abstract":["RING finger and WD repeat domain-containing protein 3 (RFWD3) is an E3 ligase known to facilitate homologous recombination by removing replication protein A (RPA) and RAD51 from DNA damage sites. Further, RPA-mediated recruitment of RFWD3 to stalled replication forks is essential for interstrand cross-link repair. Here, we report that in unperturbed human cells, RFWD3 localizes at replication forks and associates with proliferating cell nuclear antigen (PCNA) via its PCNA-interacting protein (PIP) motif. PCNA association is critical for the stability of RFWD3 and for DNA replication. Cells lacking RFWD3 show slower fork progression, a prolonged S phase, and an increase in the loading of several replication-fork components on the chromatin. These findings all point to increased frequency of"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["PCNA-mediated stabilization of E3 ligase RFWD3 at the replication fork is essential for DNA replication."],"pmcid":["PMC6310862"],"funding_grant_id":["F31 CA180616","R01 GM099669","R01 GM125196","1723008","1243372","GM099669","GM125196","1818286"],"pubmed_authors":["Hsu R","Lin YC","Prasanth KV","Arif MK","Giri S","Chakraborty A","Prasanth SG","Wang Y","Wopat S"],"additional_accession":[]},"is_claimable":false,"name":"PCNA-mediated stabilization of E3 ligase RFWD3 at the replication fork is essential for DNA replication.","description":"RING finger and WD repeat domain-containing protein 3 (RFWD3) is an E3 ligase known to facilitate homologous recombination by removing replication protein A (RPA) and RAD51 from DNA damage sites. Further, RPA-mediated recruitment of RFWD3 to stalled replication forks is essential for interstrand cross-link repair. Here, we report that in unperturbed human cells, RFWD3 localizes at replication forks and associates with proliferating cell nuclear antigen (PCNA) via its PCNA-interacting protein (PIP) motif. PCNA association is critical for the stability of RFWD3 and for DNA replication. Cells lacking RFWD3 show slower fork progression, a prolonged S phase, and an increase in the loading of several replication-fork components on the chromatin. These findings all point to increased frequency of","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Dec","modification":"2025-04-21T21:39:07.886Z","creation":"2019-09-14T07:00:57Z"},"accession":"S-EPMC6310862","cross_references":{"pubmed":["30530694"],"doi":["10.1073/pnas.1814521115"]}}