The antiviral sirtuin 3 bridges protein acetylation to mitochondrial integrity and metabolism during human cytomegalovirus infection.
Regulation of mitochondrial structure and function is a central component of infection with viruses, including human cytomegalovirus (HCMV), as a virus means to modulate cellular metabolism and immune responses. Here, we link the activity of the mitochondrial deacetylase SIRT3 and global mitochondri...
Main Authors: | Xinlei Sheng, Ileana M Cristea |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2021-04-01
|
Series: | PLoS Pathogens |
Online Access: | https://doi.org/10.1371/journal.ppat.1009506 |
Similar Items
-
Temporal dynamics of protein complex formation and dissociation during human cytomegalovirus infection
by: Yutaka Hashimoto, et al.
Published: (2020-02-01) -
Sirtuin 3 regulates mitochondrial protein acetylation and metabolism in tubular epithelial cells during renal fibrosis
by: Yu Zhang, et al.
Published: (2021-09-01) -
Sirtuin 2 promotes human cytomegalovirus replication by regulating cell cycle progression
by: Cora N. Betsinger, et al.
Published: (2023-12-01) -
Mitochondrial Sirtuins in Reproduction
by: Giovanna Di Emidio, et al.
Published: (2021-06-01) -
Inhibition of nuclear deacetylase Sirtuin-1 induces mitochondrial acetylation and calcium overload leading to cell death
by: Yue Sun, et al.
Published: (2022-07-01)