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CDK4 — FOXM1
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Wierstra et al., Biochem Biophys Res Commun 2008
:
In contrast, we now demonstrate that this LXL-motif is not required for the activation of FOXM1c by cyclin
D1/Cdk4 , cyclin E/Cdk and cyclin A/Cdk2 or for the
repression of
FOXM1c by p27
Wierstra et al., Biochem Biophys Res Commun 2013
:
Cyclin D1/Cdk4 increases the transcriptional activity of
FOXM1c without phosphorylating FOXM1c ... Anders et al. ( 2011 ) [ 11 ] reported that
cyclinD1/Cdk4 and cyclinD3/Cdk6
enhance the transcriptional activity of
FOXM1c by phosphorylating its TAD ... They defined 12 Cdk consensus sites as essential for the
activation of
FOXM1c by
cyclinD1/Cdk4 and cyclinD3/Cdk6 and stated that the 12 Cdk-sites are positioned within the TAD of FOXM1c ... This study shows that the
activation of
FOXM1c by
cyclinD1/Cdk4 is lost without removal of any cyclin/Cdk site and gained without addition of any cyclin/Cdk site because it depends on a FOXM1c domain with no potential cyclin/Cdk site, namely on the interaction domain for the tumor suppressor RB, which binds to and represses FOXM1c ...
CyclinD1/Cdk4 activates
FOXM1c because cyclinD1/Cdk4 releases FOXM1c from its repression by RB through removal of RB from FOXM1c ... For this purpose,
cyclinD1/Cdk4 phosphorylates only RB, but not FOXM1c, so that cyclinD1/Cdk4 increases the transcriptional activity of FOXM1c without phosphorylating FOXM1c and
activates FOXM1c independently of cyclin/Cdk phosphorylation sites in FOXM1c ... In summary, this study changes the model of Anders et al. ( 2011 ) [ 11 ] completely because it disproves their central conclusion that
cyclinD1/Cdk4 and cyclinD3/Cdk6
enhance the transcriptional activity of
FOXM1c by phosphorylating its TAD at the 12 Cdk-sites