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X binds VCPIP1. 22 / 22
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"The GST pulldown assay demonstrated that VCPIP1 bound to HBx directly ( xref ) in vitro ."
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"The HBx C-terminal sequence, spanning aa 121 to 154, predominated in the HBx-VCPIP1 binding, as seen in the colony abolishment in the yeast two-hybrid assay with pGBKT7-HBxΔ121–154, which lacked the sequences ( xref )."
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"These results demonstrate that the interaction between HBx and VCPIP1 may increase HBx stability."
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"Co-immunoprecipitation (Co-IP) assay using cell lysates demonstrated the association of HBx with both endogenously and exogenously expressed VCPIP1 ( xref Fig. S1), while co-IP using in vitro -translated proteins confirmed a direct binding between HBx and VCPIP1 ( xref )."
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"We, therefore, tested whether these domains were involved in VCPIP1-HBx binding."
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"The mutual interactions between VCPIP1 and HBx ( xref ), HBx and PSMC3 ( xref ), and PSMC3 and VCPIP1 ( xref ) were identified."
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"Combined with the earlier results demonstrating that HBx aa 121 to 154 and VCPIP1 aa 863 to 1221 were required for VCPIP1-HBx interaction ( xref and xref ), we narrowed down the sequence for interacting with HBx to VCPIP1 C-terminal aa 863 to 982 ( xref )."
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"First, we reported that VCPIP1 bound directly to HBx through its C-terminal aa 863 to 1221, and the interacting sequences were sufficient for HBx stability even in the absence of its N-terminal enzymatic activity."
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"Furthermore, VCPIP1-HBx interaction appears to facilitate HBx protein to exert its pleiotropic effects including canonical transactivational activity and cell proliferation inhibition, suggesting its potential role in the pathogenesis of HBV-related hepatocellular carcinoma."
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"Functionally, HBx specifically binding to VCPIP1 significantly enhanced the transcriptional transactivation of HBx by activating NF-kappaB, AP-1, and SP-1 and inhibited hepatoma cell clonogenicity in Huh7 and HepG2 cells."
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"The direct binding between VCPIP1 and HBx was verified by an in vitro glutathione S-transferase (GST) pulldown assay, and their physical interaction was validated by an in vivo coimmunoprecipitation (Co-IP) assay and confocal microscopy assay."
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"These results demonstrate that the interaction between HBx and VCPIP1 may increase HBx stability."
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"The mutual interactions between VCPIP1 and HBx (Fig. 1), HBx and PSMC3 (Fig. 5A), and PSMC3 and VCPIP1 (Fig. 5B) were identified."
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"First, we reported that VCPIP1 bound directly to HBx through its C-terminal aa 863 to 1221, and the interacting sequences were sufficient for HBx stability even in the absence of its N-terminal enzymatic activity."
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"Here, we found that VCPIP1 associated with proteasomal subunits and with HBx and prevented HBx degradation."
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"In addition, the deubiquitinating enzyme VCPIP1 binds to HBx protein and promotes stabilization of HBx in a ubiquitin-independent manner by recruiting the PSMC3 in vivo [30]."
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"In addition, the deubiquitinating enzyme VCPIP1 binds to HBx protein and promotes stabilization of HBx in a ubiquitin-independent manner by recruiting the PSMC3 in vivo [ xref ]."
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"Functionally, HBx specifically binding to VCPIP1 significantly enhanced the transcriptional transactivation of HBx by activating NF-κB, AP-1, and SP-1 and inhibited hepatoma cell clonogenicity in Huh7 and HepG2 cells."
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"We characterized the binding between VCPIP1 and HBx and noted the stabilizing effect of such binding on HBx protein, which was recently reported by another group (17)."
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"Co-immunoprecipitation (Co-IP) assay using cell lysates demonstrated the association of HBx with both endogenously and exogenously expressed VCPIP1 (Fig. 1C Fig. S1), while co-IP using in vitro-translated proteins confirmed a direct binding between HBx and VCPIP1 (Fig. 1D)."
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"In addition to the binding between VCPIP1 and HBx, an unexpected and interesting observation was also made from the co-IP results: overexpression of VCPIP1 was associated with apparently higher expression of HBx protein in the input samples (Fig. 1C, right and Fig. S1B)."
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"Regarding VCPIP1, Wu et al. used co-IP and two-hybrid assay in yeast cells and mapped HBx-binding to VCPIP1’s C-terminal region downstream of Ubl domain (17)."
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