{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Batenburg NL"],"funding":["Natural Sciences and Engineering Research Council of Canada","Canadian Institutes of Health Research","CIHR"],"pagination":["5067-5087"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11109976"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(9)"],"pubmed_abstract":["CSB (Cockayne syndrome group B) and SMARCAL1 (SWI/SNF-related, matrix-associated, actin-dependent, regulator of chromatin, subfamily A-like 1) are DNA translocases that belong to the SNF2 helicase family. They both are enriched at stalled replication forks. While SMARCAL1 is recruited by RPA32 to stalled forks, little is known about whether RPA32 also regulates CSB's association with stalled forks. Here, we report that CSB directly interacts with RPA, at least in part via a RPA32C-interacting motif within the N-terminal region of CSB. Modeling of the CSB-RPA32C interaction suggests that CSB binds the RPA32C surface previously shown to be important for binding of UNG2 and SMARCAL1. We show that this interaction is necessary for promoting fork slowing and fork degradation in BRCA2-deficient "],"journal":["Nucleic acids research"],"pubmed_title":["CSB and SMARCAL1 compete for RPA32 at stalled forks and differentially control the fate of stalled forks in BRCA2-deficient cells."],"pmcid":["PMC11109976"],"funding_grant_id":["PJT180258","RGPIN-05110","RGPIN-05490","PJT159793"],"pubmed_authors":["Batenburg NL","Zhu XD","Sowa DJ","Walker JR","Andres SN"],"additional_accession":[]},"is_claimable":false,"name":"CSB and SMARCAL1 compete for RPA32 at stalled forks and differentially control the fate of stalled forks in BRCA2-deficient cells.","description":"CSB (Cockayne syndrome group B) and SMARCAL1 (SWI/SNF-related, matrix-associated, actin-dependent, regulator of chromatin, subfamily A-like 1) are DNA translocases that belong to the SNF2 helicase family. They both are enriched at stalled replication forks. While SMARCAL1 is recruited by RPA32 to stalled forks, little is known about whether RPA32 also regulates CSB's association with stalled forks. Here, we report that CSB directly interacts with RPA, at least in part via a RPA32C-interacting motif within the N-terminal region of CSB. Modeling of the CSB-RPA32C interaction suggests that CSB binds the RPA32C surface previously shown to be important for binding of UNG2 and SMARCAL1. We show that this interaction is necessary for promoting fork slowing and fork degradation in BRCA2-deficient ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-07-15T09:19:38.711Z","creation":"2026-07-02T03:09:02.276Z"},"accession":"S-EPMC11109976","cross_references":{"pubmed":["38416570"],"doi":["10.1093/nar/gkae154"]}}