| First Author | Kim M | Year | 2016 |
| Journal | FEBS Lett | Volume | 590 |
| Issue | 3 | Pages | 340-8 |
| PubMed ID | 26783108 | Mgi Jnum | J:229978 |
| Mgi Id | MGI:5755185 | Doi | 10.1002/1873-3468.12060 |
| Citation | Kim M, et al. (2016) The role of USP1 autocleavage in DNA interstrand crosslink repair. FEBS Lett 590(3):340-8 |
| abstractText | The Fanconi anemia (FA) pathway regulates DNA interstrand crosslink (ICL) repair. A critical step in this pathway is mono-ubiquitination of FANCD2 (FANCD2-Ub). Deubiquitinase USP1 removes ubiquitin from FANCD2 resulting in inactivation of the FA pathway. USP1 is autocleaved and subsequently degraded for its down-regulation. Here, we investigated the functional consequences of Usp1-autocleavage defect. Usp1-autocleavage mutant (Usp1(GG/AA) ) corrected the level of Fancd2-Ub similar to Usp1(WT) in Usp1(-/-) MEFs. However, Usp1(GG/AA) only partially rescued MMC sensitivity with defective Fancd2 foci formation and homologous recombination defect. Contrary to this, Usp1(GG/AA) was capable of recovering UV resistance of Usp1(-/-) MEFs to a similar extent with Usp1(WT) . Taken together, our findings suggest that Usp1 regulation by autocleavage is critical for Usp1 to exert its function in ICL repair. |
