IndraLab

Statements

USP11 binds MYC. 10 / 10
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"Co-immunoprecipitation (Co-IP) of Myc-USP11 with SFB-SPRTN full-length (FL) or ΔSprT, ΔSH, ΔPIP, ΔUBZ, E112A catalytic inactive, and Y117C (SPRTN mutation identified in RJALS patients) mutant constructs showed that SPRTN-USP11 interaction was lost with deletion of the N-terminal SprT domain of SPRTN ( xref A )."
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"Indeed, we found that overexpression of Myc-USP11 FL, but not C318S catalytic inactive mutant was able to deubiquitinate SFB-SPRTN in HEK 293T cells ( xref A )."
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"We further corroborated this observation in a similar in vitro DUB reaction by incubating SFB-HA-Ub-SPRTN alone or with Myc-USP11 or Myc-USP11 C318S purified proteins and immunoblotted for HA-Ub ( xref B )."
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"We next confirmed deubiquitination of monoubiquitinated SPRTN by performing deubiquitination assays in HEK 293T cells expressing SFB-SPRTN either alone or in combination with Myc-USP11 FL or C318S mutant ( xref C ) and SFB-SPRTN and HA-Ub constructs expressed either alone or in combination with Myc-USP11 FL and C318S mutant ( xref A )."
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"As shown in Figure 4A , PB2, PA, and NP specifically co-precipitated with Myc-USP11 (lanes 3, 9, and 12, respectively)."
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"To examine the effect of USP11 on SPRTN protein stability, we expressed SFB-SPRTN E112A in combination with increasing concentrations of either Myc-USP11 or Myc-USP11 C318S mutant."
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"Co-IP experiments of SFB-SPRTN with Myc-USP11 FL and internal deletion constructs of the USP domain showed that the SPRTN interaction site resides within the 480 to 505 aa region of USP11 ( xref C )."
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"PB2-HA and Myc-USP11 were transiently co-expressed (lane 4) or singly expressed (lanes 2 and 3) in 293T cells."
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"To show that deubiquitination of SPRTN by USP11 is direct, we purified SFB-SPRTN, Myc-USP11, and Myc-USP11 C318S proteins from HEK 293T cells and performed an in vitro DUB reaction by incubating SFB-SPRTN alone or with Myc-USP11 or Myc-USP11 C318S purified proteins."
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"Co-IP experiments of SFB-SPRTN with Myc-USP11 FL, C318S catalytic inactive, ΔDUSP, and ΔUSP mutant constructs showed that SPRTN interacts with the C-terminal USP domain of USP11 ( xref B )."
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