ArticlePloS one2013
Systematic Analysis of the Functions of Lysine Acetylation in the Regulation of Tat Activity.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- QSyncFold: quantum neural network for multidimensional sync-discovery in protein folding.Briefings in bioinformatics · 2026Article
- Design and Characterization of Mutated Variants of the Oncotoxic Parvoviral Protein NS1.Viruses · 2023Article
- HIV-1 subtype C Tat exon-1 amino acid residue 24K is a signature for neurocognitive impairment.Journal of neurovirology · 2022Article
- Molecular Coevolution of Nuclear and Nucleolar Localization Signals inside the Basic Domain of HIV-1 Tat.Journal of virology · 2022Article
- Lysine acetylation of the housekeeping sigma factor enhances the activity of the RNA polymerase holoenzyme.Nucleic acids research · 2020Article
- Article
- Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019Review
- Methods for characterizing protein acetylation during viral infection.Methods in enzymology · 2019Article
- HIV latency reversing agents act through Tat post translational modifications.Retrovirology · 2018Article
- Lysine residues K66, K109, and K110 in the bovine foamy virus transactivator protein are required for transactivation and viral replication.Virologica Sinica · 2016Article
- Modulation of the stability and activities of HIV-1 Tat by its ubiquitination and carboxyl-terminal region.Cell & bioscience · 2014Article
- Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Tat protein of HIV-1 has several well-known properties, such as nucleocytoplasmic trafficking, transactivation of transcription, interaction with tubulin, regulation of mitotic progression, and induction of apoptosis. Previous studies have identified a couple of lysine residues in Tat that are essential for its functions. In order to analyze the functions of all the lysine residues in Tat, we mutated them individually to alanine, glutamine, and arginine. Through systematic analysis of the lysine mutants, we discovered several previously unidentified characteristics of Tat. We found that lysine acetylation could modulate the subcellular localization of Tat, in addition to the regulation of its transactivation activity. Our data also revealed that lysine mutations had distinct effects on microtubule assembly and Tat binding to bromodomain proteins. By correlation analysis, we further found that the effects of Tat on apoptosis and mitotic progression were not entirely attributed to its effect on microtubule assembly. Our findings suggest that Tat may regulate diverse cellular activities through binding to different proteins and that the acetylation of distinct lysine residues in Tat may modulate its interaction with various partners.
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