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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