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CDT1 — PCNA
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(physical association, affinity chromatography technology)
Nishitani et al., EMBO J 2006*
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(physical association, affinity chromatography technology)
Sugimoto et al., Mol Biol Cell 2008
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(direct interaction, pull down)
Sugimoto et al., Mol Biol Cell 2008
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(physical association, affinity chromatography technology)
Senga et al., J Biol Chem 2006*
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(physical association, affinity chromatography technology)
Hu et al., J Biol Chem 2006*
-
IRef Biogrid Interaction:
PCNA
—
CDT1
(direct interaction, pull down)
Arias et al., Nat Cell Biol 2006*
-
IRef Hprd Interaction:
PCNA
—
CDT1
(in vitro)
Senga et al., J Biol Chem 2006*, Nishitani et al., EMBO J 2006*
-
IRef Hprd Interaction:
PCNA
—
CDT1
(in vivo)
Senga et al., J Biol Chem 2006*, Nishitani et al., EMBO J 2006*
-
IRef Intact Interaction:
PCNA
—
CDT1
(physical association, pull down)
Nishitani et al., EMBO J 2006*
-
IRef Intact Interaction:
PCNA
—
CDT1
(physical association, anti bait coimmunoprecipitation)
Nishitani et al., EMBO J 2006*
Text-mined interactions from Literome
Liu et al., J Biol Chem 2004
:
These data suggest that
cyclin/Cdk mediated
Cdt1 phosphorylation is required for the association of Cdt1 with the SCF ( Skp2 ) ubiquitin ligase and thus is important for the cell cycle dependent degradation of Cdt1 in mammalian cells
Arias et al., Nat Cell Biol 2006
:
Cdt1 and DDB1 interact in extracts, and DDB1 chromatin loading is
dependent on the binding of Cdt1 to
PCNA , which indicates that PCNA docking activates the pre formed Cdt1-Cul4 ( DDB1 ) ligase complex
Hu et al., J Biol Chem 2006
:
Silencing
PCNA in cultured mammalian cells or repression of pcn1 expression in fission yeast
blocked Cdt1 degradation in response to DNA damage ... We suggest that the Cul4-Ddb1 ligase evolved to ubiquitinate Cdt1 during normal cell growth as well as in response to DNA damage and a separate E3 ligase, possibly SCF ( Skp2 ), evolved to either share or take over the function of Cdt1 ubiquitination during normal cell growth and that
PCNA is
involved in mediating
Cdt1 degradation by the Cul4-Ddb1 ligase in response to DNA damage
Higa et al., Cell cycle (Georgetown, Tex.) 2006
:
We found that
PCNA interacts with CDT1 and loss of PCNA
suppressed CDT1 proteolysis after DNA damage
Shiomi et al., Mol Cell Biol 2012
:
Two different replication factor C proteins, Ctf18 and RFC1, separately control
PCNA-CRL4Cdt2 mediated
Cdt1 proteolysis during S phase and following UV irradiation