Lysine-specific post-translational modifications of proteins in the life cycle of viruses
Loboda A. P., Sund S. M., Piacentini M., Barlev N. A.
Cell Cycle
Vol.18, Issue17, P. 1995-2005
Опубликовано: 2019
Тип ресурса: Обзор
DOI:10.1080/15384101.2019.1639305
Аннотация:
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 mechanism
Ключевые слова:
acetylation; antiviral therapy; methylation; post-translational modifications; ubiquitination; Virus trafficking
lysine; viral protein; lysine; viral protein; cell transport; covalent bond; life cycle; nonhuman; protein acetylation; protein function; protein methylation; regulatory mechanism; Review; translational protein modification; ubiquitination; virus; virus entry; virus immunity; virus neutralization; virus particle; virus replication; acetylation; genetics; human; life cycle stage; methylation; phosphorylation; protein processing; virus; Acetylation; Humans; Life Cycle Stages; Lysine; Methylation; Phosphorylation; Protein Processing, Post-Translational; Ubiquitination; Viral Proteins; Virus Replication; Viruses
Язык текста: Английский
ISSN: 1551-4005
Loboda A. P.
Sund S. M. Surinder Mokhan 1969-
Piacentini M.
Barlev N. A.
Лобода А. П.
Сунд С. М. Суриндер Мохан 1969-
Пиаcентини М.
Барлев Н. А.
Lysine-specific post-translational modifications of proteins in the life cycle of viruses
Текст визуальный непосредственный
Cell Cycle
Landes Bioscience
Vol.18, Issue17 P. 1995-2005
2019
Обзор
acetylation antiviral therapy methylation post-translational modifications ubiquitination Virus trafficking
lysine viral protein lysine viral protein cell transport covalent bond life cycle nonhuman protein acetylation protein function protein methylation regulatory mechanism Review translational protein modification ubiquitination virus virus entry virus immunity virus neutralization virus particle virus replication acetylation genetics human life cycle stage methylation phosphorylation protein processing virus Acetylation Humans Life Cycle Stages Lysine Methylation Phosphorylation Protein Processing, Post-Translational Ubiquitination Viral Proteins Virus Replication Viruses
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 mechanism