Viduth K. Chaugule

Information Published In Science Advances Volume 8 | Issue 39 September 2022 Copyright Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

Abstract Ubiquitin-specific protease 1 (USP1) acts together with the cofactor UAF1 during DNA repair processes to specifically remove monoubiquitin signals. One substrate of the USP1−UAF1 complex is the monoubiquitinated FANCI−FANCD2 heterodimer, which is involved in the repair of DNA interstrand crosslinks via the Fanconi anemia pathway. Here we determine structures of human USP1−UAF1 with and without ubiquitin and bound to monoubiquitinated FANCI−FANCD2.

RNF12 XLID Mutants Localize to the Nucleus and Dimerize Enzymes in the ubiquitin system are frequently mutated in ID, suggesting a key role for protein ubiquitylation in neural development and pathogenesis of intellectual disorders. RNF12/RLIM was identified as an XLID gene, with point mutations closely segregating with the affected males from four XLID families (Hu et al., 2016xX-exome sequencing of 405 unresolved families identifies seven novel intellectual disability genes.