{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSHLD1 is a critical component of the shieldin complex, a multiprotein assembly that controls the pathway choice during DNA double‐strand break repair by counteracting DNA end‐resection and thereby promoting non‐homologous end joining (NHEJ). Although its individual molecular activities have not been dissected in detail, SHLD1—along with its partners SHLD2, SHLD3, and MAD2L2 (REV7)—contributes to the overall integrity and function of this complex. The assembly and stabilization of shieldin depend on proper intersubunit interactions; for example, efficient MAD2L2 dimerization (a process facilitated in part by interactions with other shieldin components) is crucial for optimal assembly and subsequent recruitment of regulatory factors such as the TRIP13 ATPase, which drives essential topological switches within the complex. In this context, SHLD1 is thought to support complex stability and activity, ensuring that DNA repair is channeled away from resection-dependent homologous recombination and toward NHEJ, thus maintaining genomic integrity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Inge de Krijger, Bastian Föhr, Santiago Hernández Pérez, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MAD2L2 dimerization and TRIP13 control shieldin activity in DNA repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-021-25724-y"}], "href": "https://doi.org/10.1038/s41467-021-25724-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34521823"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34521823"}]}]}]}