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Tat
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tat
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Cullin 5 is downregulated in HIV-1 Tat and NC cotransfection of HEK 293T cells |
PubMed
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Vif
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vif
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HIV-1 Vif interacts with CUL5 |
PubMed
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vif
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Both Cul5-Rbx1 and Cul5-Rbx2 interactions promote APOBEC3G polyubiquitination in vitro and this promotion depends on the presence of the Vif-CBFbeta-EloB-EloC complex |
PubMed
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vif
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HIV-1 Vif ubiquitination is promoted by Cul5 in vitro and in vivo in a manner that requires an intact SOCS-box motif in Vif, and auto ubiquitination of Vif occurs within an assembled Vif-Cul5 complex |
PubMed
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vif
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CUL5/RBX2/ELOB/ELOC/Vif/CBF-beta complex catalyzes polyubiquitin chain formation on A3G in the presence of ubiquitin E2 UBE2R1 (CDC34) or UBCH5b (UBE2D2) |
PubMed
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vif
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HIV-1 Vif, CBF-beta, CUL5, and ELOB/C form a complex that is required for Vif-mediated downregulation of A3G and A3F. CBF-beta regulates HIV-1 infectivity only in the presence of A3G |
PubMed
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vif
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Two highly conserved Cys residues (C114 and C133) outside the SOCS box (amino acids 144-169) motif in HIV-1 Vif are required for the interaction of Vif with Cul5 but not ElonginC |
PubMed
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vif
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HIV-1 Vif (amino acids 144-149; SLQXLA motif; BC-box) interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-Cullin-F-box (SCF)-like complex that allows Vif to interact with APOBEC3G and induce its ubiquitination and degradation |
PubMed
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vif
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Amino-acid motifs 84GxSIEW89 and 102LADQLI107 in HIV-1 Vif affect its interaction with CUL5, and Vif mutants 84DVAAAA89, 88EW/AA89, G84A, G84D, W89A, S104A, L106S, and I107S have more than 50% reduction in CUL5 binding |
PubMed
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vif
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UBE2F and RBX2 are required for activation of the polyubiquitin synthesis activity of Vif/CBF-beta/CUL5, leading to HIV-1 Vif-mediated degradation of A3G in cells |
PubMed
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vif
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The T(Q/D/E)x(5)ADx(2)(I/L) motif, located at residues 96 to 107 in HIV-1 Vif, regulates Vif interaction with Cul5 |
PubMed
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vif
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Simultaneous substitution of the three Vif-interacting residues L52, W53, and D55 and the two ELOC-interacting residues P41 and H48 in CUL5 impairs the ability of CUL5 to interact with the Vif-CBF-beta-ELOB-ELOC protein complex |
PubMed
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vif
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The absence of Vif-CBF-beta reduces the interaction between the CUL5 and the EloC-EloB complex, indicating that the former two proteins have a critical role in promoting assembly of the pentameric complex |
PubMed
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vif
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An overall crystal structure indicates that the Vif-CBF-beta-CUL5-ELOB-ELOC complex has a U-shape architecture, including the two straight arms Vif-CBF-beta and CUL5 and the bent arm formation between ELOC and CUL5 and Vif interactions |
PubMed
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vif
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The interaction between Cul5 and HIV-1, HIV-2, SIVmac, or SIVagm Vif protein require the presence of zinc |
PubMed
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vif
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The HIV-1 Vif N-terminal motif (residues 18-38) binds CUL5 in mammalian cells and is reguired for A3F and A3G degradation and HIV-1 infectivity |
PubMed
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vif
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HIV-1 Vif mutants C114S and C133A abolish the interaction with CUL5, which leads to fail to A3G degradation by Vif |
PubMed
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vif
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HIV-1 Vif YF111/112AA, F115A, I120S and AL123/124SS mutants are unable to recruit Cul5, but retain interactions with Elongin B and C proteins |
PubMed
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vif
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Deletion of amino acids 120 to 138 in Cul5 significantly reduces its interaction with HIV-1 Vif, but does not affect Cul5 binding to Elongins B/C; the HCCH zinc-binding motif (residues 108-139) in Vif is required for the interaction with Cul5 |
PubMed
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vif
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The interaction between the HIV-1 Vif PPLP motif (residues 161-164) and the 34-amino-acid C-terminal tail (residues 85-118) of EloB plays a role in promoting recruitment of CBF-beta to the Vif-Cul5 E3 complex |
PubMed
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vif
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The conjugation of NEDD8 to Cullin-5 by UBE2F is required for HIV-1 Vif-mediated A3G degradation |
PubMed
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vif
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CBF-beta and the N-terminal half of HIV-1 Vif enhance the affinity of Cul5 for Vif |
PubMed
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vif
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HIV-1 Vif-induced G2 accumulation requires a Cul5-based E3 ligase, but is independent of APOBEC3D/E, F, and G expression. Overexpression of ubiquitin(K48R) abolishes Vif-induced G2 accumulation |
PubMed
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vif
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Mutations in HIV-1 Vif PPLP motif (amino acids 161-164) reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5 |
PubMed
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vif
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Chim3, corresponding to amino acids 126-170 of the natural mutant F12-Vif, interacts poorly with Cul5 but affects HIV-1 Vif/Cul5 interaction |
PubMed
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vif
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Vif-induced ubiquitination of A3G and A3G20K/R is inhibited by Cul5deltaNedd8 |
PubMed
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vif
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HIV-1 Vif is regulated by Cullin5 E3 ligase and its expression levels increases in the presence of a Cullin5 dominant negative mutant, Cul5deltaNedd8 |
PubMed
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vif
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The amino acids L163 and L169 located downstream of the SOCS-box motif in HIV-1 Vif are required for Vif function and efficient interaction with Cul5-ElonginB-ElonginC |
PubMed
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vif
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Treatment with the membrane-permeable zinc chelator TPEN prevents Vif function, and causes the blockage of Cul5 recruitment and APOBEC3G (A3G) degradation |
PubMed
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nucleocapsid
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gag
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Cullin 5 is downregulated in HIV-1 Tat and NC cotransfection of HEK 293T cells |
PubMed
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