IndraLab

Statements

USP46 binds DTL. 9 / 9
| 9
sparser
"If the interaction of USP46 with Cdt2 is essential for the stabilization of Cdt2, we would expect that the residues of E6 required to stabilize Cdt2 are also essential to promote the interaction of USP46 with Cdt2."
30415951
sparser
"Only high risk but not low risk E6 proteins could promote Cdt2 interaction with USP46 and stabilize Cdt2."
30415951
sparser
"In contrast, Flag-Cdt2 alone from cells without E6 did not co-immunoprecipitate endogenous USP46 ( xref , lane 1), suggesting that Cdt2 and USP46 do not interact with each other in the absence of E6."
30415951
sparser
"Immunoprecipitation of Cdt2 and immunoblotting of the precipitate for USP46 showed that high risk 16E6 and the 1–43 fragment of 16E6, but not low risk 6E6 or 16E6-F2V/P5R, promoted the interaction of USP46 and Cdt2 ( xref ), demonstrating the correlation expected above."
30415951
sparser
"Thus, HPV E6 binds directly to USP46, and this facilitates the interaction of USP46 with its potential substrate Cdt2."
30415951
sparser
"Immunoprecipitation of endogenous cellular Cdt2 coimmunoprecipitated cellular USP46 and E6 only from HeLa cell lysates (that contain HPV E6) but not from U2OS cell lysates (that do not contain E6) ( xref ; xref ), suggesting that E6 is necessary to promote the interaction of Cdt2 with USP46."
30415951
sparser
"E6 protein promotes the interaction of USP46 with Cdt2."
30415951
sparser
"Therefore although our co-immunoprecipitation experiments showed that DDB1 is present in the USP46:Cdt2 complex [ xref ], neither DDB1 nor a substrate of the CRL4-Cdt2 complex is required for the E6:USP46:Cdt2 interaction and subsequent Cdt2 stabilization"
35008200
sparser
"Thus there was a perfect correlation between an E6 variant’s ability to bind USP46 and promote the interaction of USP46 with Cdt2, and the ability of the variant to stabilize Cdt2."
30415951