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Envelope surface glycoprotein gp120
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env
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Tandem affinity purification and mass spectrometry analysis identify subunit alpha 1a of tubulin (TUBA1A), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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env
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The binding of HIV-1 gp120 to CD4+-permissive cells increases the level of acetylated alpha-tubulin in a CD4-dependent manner; overexpression of Histone Deacetylase 6 (HDAC6) inhibits the acetylation of alpha-tubulin and prevents HIV-1-cell fusion |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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Expression of HIV-1 gp41 cytoplasmic domain reduces acetylated tubulin alpha and interferes with virus-cell fusion |
PubMed
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Gag-Pol
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gag-pol
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Tandem affinity purification and mass spectrometry analysis identify subunit alpha 1a of tubulin (TUBA1A), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Nef
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nef
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Tandem affinity purification and mass spectrometry analysis identify subunit alpha 1a of tubulin (TUBA1A), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
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Pr55(Gag)
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gag
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Tandem affinity purification and mass spectrometry analysis identify subunit alpha 1a of tubulin (TUBA1A), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
|
gag
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Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 |
PubMed
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Rev
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rev
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HIV-1 Rev interacting protein, tubulin alpha 1a (TUBA1A), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells |
PubMed
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rev
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Rev acts to depolymerize microtubules that are formed by tubulin, an effect that is observed during HIV-1 infection |
PubMed
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Tat
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tat
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HIV-1 Tat K29A, K50R, and K51R lysine mutations downregulate the proportion of soluble tubulin in cells, while the majority of other lysine mutations upregulate the percentage of soluble tubulin compared with the wild-type |
PubMed
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tat
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HIV-1 Tat (specifically, amino acids 38-72), enhances tubulin polymerization and triggers the mitochondrial pathway to induce T cell apoptosis as shown in vitro by the release of cytochrome c from isolated mitochondria |
PubMed
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tat
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HIV-1 Tat causes a dramatic decrease in alpha-tubulin staining, which indicates disruption of the cytoskeleton organization in human intestinal epithelial cells |
PubMed
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tat
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HIV-1 Tat (amino acids 36-39) binds tubulin alpha/beta dimers and polymerized microtubules leading to the alteration of microtubule dynamics and activation of a mitochondria-dependent apoptotic pathway that is facilitated by the Bcl-2 relative Bim |
PubMed
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integrase
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gag-pol
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Co-immunoprecipitation shows interaction of HIV-1 IN with alpha-tubulin |
PubMed
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