Journal
JOURNAL OF CELL BIOLOGY
Volume 194, Issue 2, Pages 177-186Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201101062
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Funding
- National Institutes of Health [R01-GM084244, R01-GM057587, R37-CA076584, R21-CA161108]
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Targeted protein destruction of critical cellular regulators during the G1 phase of the cell cycle is achieved by anaphase-promoting complex/cyclosome(Cdh1) (APC/C-Cdh1), a multisubunit E3 ubiquitin ligase. Cells lacking Cdh1 have been shown to accumulate deoxyribonucleic acid (DNA) damage, suggesting that it may play a previously unrecognized role in maintaining genomic stability. The ubiquitin-specific protease 1 (USP1) is a known critical regulator of DNA repair and genomic stability. In this paper, we report that USP1 was degraded in G1 via APC/C-Cdh1. USP1 levels were kept low in G1 to provide a permissive condition for inducing proliferating cell nuclear antigen (PCNA) monoubiquitination in response to ultraviolet (UV) damage before DNA replication. Importantly, expression of a USP1 mutant that cannot be degraded via APC/C-Cdh1 inhibited PCNA monoubiquitination during G1, likely compromising the recruitment of trans-lesion synthesis polymerase to UV repair sites. Thus, we propose a role for APC/C-Cdh1 in modulating the status of PCNA monoubiquitination and UV DNA repair before S phase entry.
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