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Manipulation of the host protein acetylation network by human immunodeficiency virus type 1.

ABSTRACT: Over the past 15 years, protein acetylation has emerged as a globally important post-translational modification that fine-tunes major cellular processes in many life forms. This dynamic regulatory system is critical both for complex eukaryotic cells and for the viruses that infect them. HIV-1 accesses the host acetylation network by interacting with several key enzymes, thereby promoting infection at multiple steps during the viral life cycle. Inhibitors of host histone deacetylases and bromodomain-containing proteins are now being pursued as therapeutic strategies to enhance current antiretroviral treatment. As more acetylation-targeting compounds are reaching clinical trials, it is time to review the role of reversible protein acetylation in HIV-infected CD4(+) T cells.

SUBMITTER: Jeng MY

PROVIDER: S-EPMC4816045 | biostudies-literature | 2015 Jul-Aug

REPOSITORIES: biostudies-literature

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Manipulation of the host protein acetylation network by human immunodeficiency virus type 1.

Jeng Mark Y MY Ali Ibraheem I Ott Melanie M

Critical reviews in biochemistry and molecular biology 20150701 4

Over the past 15 years, protein acetylation has emerged as a globally important post-translational modification that fine-tunes major cellular processes in many life forms. This dynamic regulatory system is critical both for complex eukaryotic cells and for the viruses that infect them. HIV-1 accesses the host acetylation network by interacting with several key enzymes, thereby promoting infection at multiple steps during the viral life cycle. Inhibitors of host histone deacetylases and bromodom ...[more]

PMID: 26329395

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