ArticleRetrovirology2008
Modulation of microtubule assembly by the HIV-1 Tat protein is strongly dependent on zinc binding to Tat.
Article in Retrovirology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019Review
- HIV, Tat and dopamine transmission.Neurobiology of disease · 2017Review
- Functional roles of HIV-1 Tat protein in the nucleus.Cellular and molecular life sciences : CMLS · 2016Review
- Modulation of the stability and activities of HIV-1 Tat by its ubiquitination and carboxyl-terminal region.Cell & bioscience · 2014Article
- A comparative analysis of mitochondrial ORFans: new clues on their origin and role in species with doubly uniparental inheritance of mitochondria.Genome biology and evolution · 2013Article
- Comparative nucleic acid chaperone properties of the nucleocapsid protein NCp7 and Tat protein of HIV-1.Virus research · 2012Review
- Genetic features of cerebrospinal fluid-derived subtype B HIV-1 tat.Journal of neurovirology · 2012Article
- Differential induction of rat neuronal excitotoxic cell death by human immunodeficiency virus type 1 clade B and C tat proteins.AIDS research and human retroviruses · 2011Article
- Neurodegenerative effects of recombinant HIV-1 Tat(1-86) are associated with inhibition of microtubule formation and oxidative stress-related reductions in microtubule-associated protein-2(a,b).Neurochemical research · 2011Article
- Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6.The Journal of biological chemistry · 2011Article
- Mitochondria and viruses.Mitochondrion · 2011Review
- Modifications in host cell cytoskeleton structure and function mediated by intracellular HIV-1 Tat protein are greatly dependent on the second coding exon.Nucleic acids research · 2010Article
- Attenuated neurotoxicity of the transactivation-defective HIV-1 Tat protein in hippocampal cell cultures.Experimental neurology · 2009Article
- What does the structure-function relationship of the HIV-1 Tat protein teach us about developing an AIDS vaccine?Retrovirology · 2009Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDuring HIV-1 infection, the Tat protein plays a key role by transactivating the transcription of the HIV-1 proviral DNA. In addition, Tat induces apoptosis of non-infected T lymphocytes, leading to a massive loss of immune competence. This apoptosis is notably mediated by the interaction of Tat with microtubules, which are dynamic components essential for cell structure and division. Tat binds two Zn2+ ions through its conserved cysteine-rich region in vitro, but the role of zinc in the structure and properties of Tat is still controversial.
resultsTo investigate the role of zinc, we first characterized Tat apo- and holo-forms by fluorescence correlation spectroscopy and time-resolved fluorescence spectroscopy. Both of the Tat forms are monomeric and poorly folded but differ by local conformational changes in the vicinity of the cysteine-rich region. The interaction of the two Tat forms with tubulin dimers and microtubules was monitored by analytical ultracentrifugation, turbidity measurements and electron microscopy. At 20 degrees C, both of the Tat forms bind tubulin dimers, but only the holo-Tat was found to form discrete complexes. At 37 degrees C, both forms promoted the nucleation and increased the elongation rates of tubulin assembly. However, only the holo-Tat increased the amount of microtubules, decreased the tubulin critical concentration, and stabilized the microtubules. In contrast, apo-Tat induced a large amount of tubulin aggregates.
conclusionOur data suggest that holo-Tat corresponds to the active form, responsible for the Tat-mediated apoptosis.
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