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• W2024053451 abstract "During the late phase of the Human Immunodeficiency Virus Type-1 (HIV-1) replication cycle, viral Gag proteins and the intact RNA genome are trafficked to specific sub-cellular membranes where virus assembly and budding occurs. Targeting to the plasma membranes of T cells and macrophages is mediated by interactions between the N-terminal matrix (MA) domain of Gag and cellular phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] molecules. However, in macrophages and dendritic cells, a subset of Gag proteins appears to be targeted to tetraspanin enriched viral compartments, a process that appears to be mediated by MA interactions with the Delta subunit of the cellular Adaptor Protein AP-3 (AP-3δ). We cloned, overexpressed and purified the protein interactive domain of AP-3δ and probed for MA binding by NMR. Unexpectedly, no evidence of binding was observed in these in vitro experiments, even at relatively high protein concentrations (200 μM), suggesting that AP-3δ plays an alternative role in HIV-1 assembly." @default.
• W2024053451 created "2016-06-24" @default.
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• W2024053451 date "2012-11-01" @default.
• W2024053451 modified "2023-09-27" @default.
• W2024053451 title "The HIV-1 matrix protein does not interact directly with the protein interactive domain of AP-3δ" @default.
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• W2024053451 doi "https://doi.org/10.1016/j.virusres.2012.06.007" @default.
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