Ontology highlight
ABSTRACT: Importance
This study expands the growing understanding that protein acetylation is a highly regulated molecular toggle of protein function in both host anti-viral defense and viral replication. We describe a pro-viral role for the human enzyme SIRT2, showing that its deacetylase activity supports HCMV replication. By integrating quantitative proteomics, flow cytometry cell cycle assays, microscopy, and functional virology assays, we investigate the temporality of SIRT2 functions and substrates. We identify a pro-viral role for the SIRT2 deacetylase activity via regulation of CDK2 K6 acetylation and the G1-S cell cycle transition. These findings highlight a link between viral infection, protein acetylation, and cell cycle progression.
SUBMITTER: Betsinger CN
PROVIDER: S-EPMC10734535 | biostudies-literature | 2023 Dec
REPOSITORIES: biostudies-literature
Betsinger Cora N CN Justice Joshua L JL Tyl Matthew D MD Edgar Julia E JE Budayeva Hanna G HG Abu Yaa F YF Cristea Ileana M IM
mSystems 20231102 6
<h4>Importance</h4>This study expands the growing understanding that protein acetylation is a highly regulated molecular toggle of protein function in both host anti-viral defense and viral replication. We describe a pro-viral role for the human enzyme SIRT2, showing that its deacetylase activity supports HCMV replication. By integrating quantitative proteomics, flow cytometry cell cycle assays, microscopy, and functional virology assays, we investigate the temporality of SIRT2 functions and sub ...[more]