<HashMap><database>bioimages</database><scores/><additional><omics_type>Unknown</omics_type><submitter/><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-BIAD885</full_dataset_link><repository>bioimages</repository><figure_sub>Specimen</figure_sub><figure_sub>Image analysis</figure_sub><figure_sub>Study Component</figure_sub><figure_sub>organisation</figure_sub><figure_sub>Biosample</figure_sub><figure_sub>Associations</figure_sub><figure_sub>Image acquisition</figure_sub><pubmed_authors>Image Data Resource (IDR)</pubmed_authors></additional><is_claimable>false</is_claimable><name>High content screen for genes whose downregulation by RNAi affects acccumulation of p53-binding protein 1 (53BP1) at sites of double strand breaks (OME-NGFF)</name><description>OME-NGFF converted study from idr0010.  DNA double-strand breaks (DSBs) not only interrupt the genetic information, but also disrupt the chromatin structure, and both impairments require repair mechanisms to ensure genome integrity. We showed previously that RNF8-mediated chromatin ubiquitylation protects genome integrity by promoting the accumulation of repair factors at DSBs. Here, we provide evidence that, while RNF8 is necessary to trigger the DSB-associated ubiquitylations, it is not sufficient to sustain conjugated ubiquitin in this compartment. We identified RNF168 as a novel chromatin-associated ubiquitin ligase with an ability to bind ubiquitin. We show that RNF168 interacts with ubiquitylated H2A, assembles at DSBs in an RNF8-dependent manner, and, by targeting H2A and H2AX, ampl</description><dates><release>2023-09-06T00:00:00Z</release><modification>2024-02-06T14:17:37.12Z</modification><creation>2023-09-06T15:57:04.634Z</creation></dates><accession>S-BIAD885</accession><cross_references/></HashMap>