IndraLab

Statements

FOSL1 binds UCHL3. 5 / 5
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sparser
"Together, these findings suggest that IKKα-dependent phosphorylation facilitates the interaction between FOSL1 and UCHL3, thereby promoting FOSL1 stabilization."
41608585
sparser
"Co-IP assays further validated the interaction between FOSL1 and UCHL3 in GBM cells ( xref A-B), and GST-pull-down assays using purified GST-FOSL1 and His-UCHL3 proteins substantiated their direct binding (Figure xref C)."
41608585
sparser
"Notably, IKKα-mediated phosphorylation of FOSL1 strengthened its association with UCHL3, as evidenced by diminished UCHL3-FOSL1 binding upon mutation of the phosphorylation site, supporting a phosphorylation-dependent recruitment mechanism that safeguards FOSL1 stability."
41608585
sparser
"To determine whether IKKα-mediated phosphorylation modulates the interaction between FOSL1 and UCHL3, various FOSL1 mutants were expressed in HEK293T cells."
41608585
sparser
"First, although the functional interplay among FOSL1, IKKα, and UCHL3 has been delineated, the precise molecular mechanism through which IKKα enhances UCHL3 binding to FOSL1 remains incompletely understood."
41608585