c-Jun N-terminal kinase–mediated Rad18 phosphorylation facilitates Polη recruitment to stalled replication forks
Abstract
The E3 ubiquitin ligase Rad18 chaperones DNA polymerase η (Polη) to sites of UV-induced DNA damage and monoubiquitinates proliferating cell nuclear antigen (PCNA), facilitating engagement of Polη with stalled replication forks and promoting translesion synthesis (TLS). It is unclear how Rad18 activities are coordinated with other elements of the DNA damage response. We show here that Ser-409 residing in the Polη-binding motif of Rad18 is...
Paper Details
Title
c-Jun N-terminal kinase–mediated Rad18 phosphorylation facilitates Polη recruitment to stalled replication forks
Published Date
May 15, 2012
Volume
23
Issue
10
Pages
1943 - 1954
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