Skip to main page content
U.S. flag

An official website of the United States government

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2019 Sep;18(17):1995-2005.
doi: 10.1080/15384101.2019.1639305. Epub 2019 Jul 10.

Lysine-specific post-translational modifications of proteins in the life cycle of viruses

Anna P Loboda  1 , Surinder M Soond  2 , Mauro Piacentini  3 , Nickolai A Barlev  1   3
Affiliations
Review

Lysine-specific post-translational modifications of proteins in the life cycle of viruses

Anna P Loboda et al. Cell Cycle. 2019 Sep.

Abstract

The process of protein post-translational modifications (PTM) is one of the critical mechanisms of regulation of many cellular processes, which makes it an attractive target for various viruses. Since viruses cannot replicate on their own, they have developed unique abilities to alter metabolic and signaling cell pathways, including protein PTMs, to ensure faithful replication of their genomes. This review describes several ways of how lysine-specific PTMs are used by various viruses to ensure its successful invasion and replication. Covalent modifications like acetylation, ubiquitination, and methylation form a complex system of reversible and often competing modifications, which adds an additional level of complexity to the system of regulation of the activity of host proteins involved in viral replication and propagation. In furthering these, we also describe the manner in which PTM pathways can also be accosted by various types of viruses to neutralize the host's cellular mechanisms for anti-viral protection and highlight key areas for future therapeutic targeting and design.

Keywords: Virus trafficking; acetylation; antiviral therapy; methylation; post-translational modifications; ubiquitination.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Lee MJ, Lee JH, Rubinsztein DC.. Tau degradation: the ubiquitin – proteasome system versus the autophagy-lysosome system. Prog Neurobiol. 2013;105:49–59. - PubMed
    1. Lee KE, Heo JE, Kim JM, et al. N-terminal acetylation-targeted N-end rule proteolytic system: the Ac/N-end rule pathway. Mol Cells. 2016;39(3):169. - PMC - PubMed
    1. Bergink S, Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature. 2009;458(7237):461. - PubMed
    1. Boisvert FM, Déry U, Masson JY, et al. Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control. Genes Dev. 2005;19(6):671–676. - PMC - PubMed
    1. Gong F, Miller KM. Mammalian DNA repair: HATs and HDACs make their mark through histone acetylation. Mutat Res. 2013;750(1–2):23–30. - PubMed

Publication types

Grants and funding

This work was funded by RFBR grant #18-29-09144 to N.B. and the grant from the Russian Government Program for the Recruitment of the leading scientists into the Russian Institutions of Higher Education 14. W03.31.0029 to N.B. and M.P.

LinkOut - more resources