Ontology highlight
ABSTRACT:
SUBMITTER: Kucej M
PROVIDER: S-EPMC5703050 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Kucej Martin M Fermaintt Charles S CS Yang Kun K Irizarry-Caro Ricardo A RA Yan Nan N
Cell reports 20170301 11
TREX1 mutations are associated with several autoimmune and inflammatory diseases. The N-terminal DNase domain of TREX1 is important for preventing self-DNA from activating the interferon response. The C terminus of TREX1 is required for ER localization and regulation of oligosacchariyltransferase (OST) activity. Here, we show that during mitosis TREX1 is predominately phosphorylated at the C-terminal Serine-261 by Cyclin B/CDK1. TREX1 is dephosphorylated quickly at mitotic exit, likely by PP1/PP ...[more]