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- W2792960739 abstract "HIV Nef downregulates cell surface host proteins, including SERINCs, CD4, and MHC-I, by redirecting them into clathrin coated vesicles (CCVs) for lysosomal degradation. Nef achieves this by hijacking the AP-1 and AP-2 clathrin adaptors. HIV-1 Nef cooperates with the host GTPase Arf1 to induce oligomerization and activation of AP-1, assembling as trimers in vitro. AP complexes’ normal function is to sort two main classes of cargo proteins into CCVs. These cargo classes are defined by the presence of a tyrosine-based YXXΦ motif or an acidic-dileucine motif [DE]XXXL[LI]. Nef-induced downregulation of MHC-I involves the hijacking of both the tyrosine and dileucine cargo binding sites of AP-1. Arf1 promotes dimerization of AP-1, while in the presence of Arf1 and Nef together, AP-1 trimers predominate. The combination of dimer and trimer interfaces lead to formation of a hexagonal lattice. In order to determine the contribution of the Nef dileucine motif to trimerization, a cryo-EM analysis of the AP-1:Arf1:NefLLAA complex was carried out. From this analysis, we conclude that the dileucine motif of Nef is important for promoting trimerization of the Arf1:AP-1 clathrin adaptor complex and subsequent clathrin cage assembly." @default.
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- W2792960739 date "2018-02-01" @default.
- W2792960739 modified "2023-09-28" @default.
- W2792960739 title "Role of the Dileucine Motif in Nef-Induced Trimerization of the ARF1:AP-1 Clathrin Adaptor Complex" @default.
- W2792960739 doi "https://doi.org/10.1016/j.bpj.2017.11.3117" @default.
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