期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
卷 1865, 期 7, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bbagrm.2022.194859
关键词
Bromodomain; ET domain; BET; BRD4; Virus; Acetylation; Mechanism
资金
- NIH [HL151334, CA252707, GM125195, GM135671, AG067664, AI129745, CA250459, AI137270, AI083139]
This article discusses the pathological functions of BET proteins during viral infection, focusing on the mechanisms underlying their direct interactions with viral proteins.
Viruses use diverse tactics to hijack host cellular machineries to evade innate immune responses and maintain their life cycles. Being critical transcriptional regulators, human BET proteins are prominent targets of a growing number of viruses. The BET proteins associate with chromatin through the interaction of their bromodomains with acetylated histones, whereas the carboxy-terminal domains of these proteins contain docking sites for various human co-transcriptional regulators. The same docking sites however can be occupied by viral proteins that exploit the BET proteins to anchor their genome components to chromatin in the infected host cell. In this review we highlight the pathological functions of the BET proteins upon viral infection, focusing on the mech-anisms underlying their direct interactions with viral proteins, such as the envelope protein from SARS-CoV-2.
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