IndraLab

Statements

USP43 binds E2F1. 11 / 11
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sparser
"These findings conclusively indicate a physical interaction between USP43 and E2F1."
41437393
sparser
"Consequently, GEM does not appear to increase USP43-E2F1 binding per se, but rather acts upstream by elevating USP43 levels, which then contributes to sustaining E2F1 protein stability."
41437393
sparser
"A set of truncated mutant plasmids was constructed for subsequent co-IP experiments to delve deeper into the specific structural domains involved in the binding of USP43 and E2F1."
41437393
sparser
"USP43 interacts with E2F1, removing its ubiquitin tags and thereby preventing its degradation through the ubiquitin-proteasome pathway."
41437393
sparser
"As shown in Fig. xref H-K, USP43 bound to the C-terminal domain of E2F1, whereas E2F1 interacted with both the USP43-N2 and USP43-C2 regions of USP43."
41437393
sparser
"To validate USP43-E2F1 interaction, a Co-IP assay was conducted."
41437393
sparser
"After demonstrating that USP43 interacts with E2F1, we wanted to further clarify that USP43 functions as a deubiquitinase (DUB) for E2F1."
41437393
sparser
"We then proceeded to explore whether GEM stimulation affects the binding of both USP43 and E2F1."
41437393
sparser
"However, USP43 interacts with E2F1 to promote its deubiquitination and is indispensable for the GEM-induced upregulation of E2F1."
41437393
sparser
"USP43 interacts with E2F1."
41437393
sparser
"Additionally, endogenous USP43 also interacted with E2F1 in T24 and UM-UC-3 cells (Fig. xref G)."
41437393