IndraLab

Statements

USP15 binds nef. 21 / 21
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"Our data showed that Nef was detected in lane 2 together with USP15, but not in lane 1 ( xref ), indicating that Nef associated with USP15 and suggesting that Nef could be important to UPS-mediated proteosomal degradation processes."
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"Accordingly, we constructed two deletion mutants of USP15, USP15ΔN and USP15ΔC ( xref ), and examined binding of Nef to the mutant USP15 and its consequence to the reciprocal decay of mutant USP15 and Nef."
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"We next investigated whether direct interactions between Nef and USP15 are essential for the observed reciprocal decay of the proteins."
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"We then investigated whether the interaction between USP15 and Nef is required for the observed mutual degradation. xref showed that the amounts of the expressed USP15 and USP15ΔN which interact with Nef gradually declined as the amount of Nef was increased."
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"Direct interaction between Nef and USP15 was essential for the observed reciprocal decay of the proteins."
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"Direct interaction between Nef and USP15 was essential for the observed reciprocal decay of the proteins."
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"Immunoprecipitation of USP15 and its mutant proteins with anti-Myc antibody, followed by WB with anti-GFP antibody for the detection of Nef.GFP and GFP, showed that Nef.GFP, not GFP, was detected only[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Similarly, the amount of Nef was least in the cells transfected with pUSP15, as well as less in the cells transfected with pUSP15ΔN than in the cells transfected with pUSP15ΔC ( xref ), establishing that interaction of USP15 and Nef is essential for the reciprocal protein decay."
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"Similarly, the amount of Nef was least in the cells transfected with pUSP15, as well as less in the cells transfected with pUSP15DeltaN than in the cells transfected with pUSP15DeltaC, establishing th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The interaction between Nef and USP15 leads to reciprocal decay of the proteins, and the balance of USP15/Nef interplay underlines the dynamic competition between the virus and the infected host cells [101]."
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"Similarly, the amount of Nef was least in the cells transfected with pUSP15, as well as less in the cells transfected with pUSP15DeltaN than in the cells transfected with pUSP15DeltaC (XREF_FIG), establishing that interaction of USP15 and Nef is essential for the reciprocal protein decay."
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"However, Gag did not degrade USP15, indicating that the Nef and USP15 complex, in distinction to other viral proteins, play an integral role in coordinating viral protein degradation and hence HIV-1 replication."
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"Alternatively, USP15 could activate other cellular protein (s) in the USP15 and Nef complex, and the activated protein (s) in turn degrades Nef protein."
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"Conversely, the interaction between USP15 and the HIV-1 Gag and Nef (necessary for AIDS pathogenicity) inhibits HIV-1 replication."
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"We found that Nef binds to ubiquitin-protein ligase E3A (UBE3A/E6AP) which induces protein degradation by attaching Ub to substrates ( xref ; xref ), i.e. Nef associated with two functionally antagonistic proteins in the UPS-mediated protein degradation processes, suggesting that UBE3A could be a major cellular component in regulating USP15-mediated viral protein degradation by interacting with Nef and USP15 simultaneously or independently."
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"GFP, not GFP, was detected only in the cells transfected with wild type- or USPΔN-, but not with USPΔC-expressing plasmids ( xref bottom panel), indicating that Nef binds USP15 through the encoded protein motif(s) from amino acid 385 to the end of the USP15 gene."
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"To confirm association of USP15 with Nef, 293T cells were transfected with pUSP15 (lane 1) or with pHNef and pUSP15 (lane 2), and proteins from the transfected cells were precipitated with anti-USP15 Ab followed by WB with anti-USP15 first and the same blot with anti-Myc Ab again."
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"We next investigated whether direct interactions between Nef and USP15 are essential for the observed reciprocal decay of the proteins."
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"Immunoprecipitation of USP15 and its mutant proteins with anti-Myc antibody, followed by WB with anti-GFP antibody for the detection of Nef.GFP and GFP, showed that Nef.GFP, not GFP, was detected only in the cells transfected with wild type- or USPDeltaN-, but not with USPDeltaC expressing plasmids (XREF_FIG bottom panel), indicating that Nef binds USP15 through the encoded protein motif (s) from amino acid 385 to the end of the USP15 gene."
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"Association of Nef with USP15 is critical for the reciprocal regulation of decays of the proteins."
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"We then investigated whether the interaction between USP15 and Nef is required for the observed mutual degradation."
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