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CDK2 — SKP2

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: CDK2 → SKP2 (increases, SKP2 Activity) Mamillapalli et al., Curr Biol 2001*
  Evidence: Recently, we and others have identified an ubiquitin E3 ligase, the SCF(SKP2) complex, that mediates p27 ubiquitin-dependent proteolysis [5-7]. Here we report that PTEN and the PI 3-kinase pathway regulate p27 protein stability.We found that ectopic expression of SKP2 alone is sufficient to reverse PTEN-induced p27 accumulation, restore the kinase activity of cyclin E/CDK2, and partially overcome the PTEN-induced G1 cell cycle arrest.
• KEGG Cell cycle: Complex of CUL1-RBX1-SKP1-SKP2 → Complex of CCNE1-CCNE2-CDK2 (protein-protein, inhibition)
  
• Reactome Reaction: CDK2 → SKP2 (reaction) Tsvetkov et al., Curr Biol 1999, Ganoth et al., Nat Cell Biol 2001, Zhu et al., Mol Cell Biol 2004, Hao et al., Mol Cell 2005
• Reactome Reaction: CDK2 → SKP2 (indirect_complex) Tsvetkov et al., Curr Biol 1999, Ganoth et al., Nat Cell Biol 2001, Zhu et al., Mol Cell Biol 2004, Hao et al., Mol Cell 2005

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Gao et al., Nat Cell Biol 2009*
• IRef Biogrid Interaction: SKP2 — CDK2 (direct interaction, pull down) Marti et al., Nat Cell Biol 1999*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Yam et al., Mol Cell Biol 1999*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Calvisi et al., Gastroenterology 2009
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Bashir et al., Cell cycle (Georgetown, Tex.) 2010*
• IRef Biogrid Interaction: SKP2 — CDK2 (association, x-ray crystallography) Yao et al., J Mol Biol 2006*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Rosner et al., Amino Acids 2009*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Lyapina et al., Proc Natl Acad Sci U S A 1998*
• IRef Biogrid Interaction: SKP2 — CDK2 (direct interaction, pull down) Zhang et al., Cell 1995*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Zhang et al., Cell 1995*
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Inuzuka et al., Cell 2012
• IRef Biogrid Interaction: SKP2 — CDK2 (physical association, affinity chromatography technology) Varjosalo et al., Nat Methods 2013
• MIPS CORUM p27-cyclinE-Cdk2 - Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1) complex: p27-cyclinE-Cdk2 - Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1) complex complex (CCNE1-CDK2-CDKN1B-CKS1B-CUL1-RBX1-SKP1-SKP2) Xu et al., J Biol Chem 2007
• IRef Corum Interaction: Complex of RBX1-SKP1-CKS1B-CDKN1B-CDK2-CCNE1-SKP2-CUL1 (association, anti tag coimmunoprecipitation) Xu et al., J Biol Chem 2007
• IRef Hprd Interaction: SKP2 — CDK2 (in vivo) Bilodeau et al., FEBS Lett 1999*
• IRef Intact Interaction: Complex of CDK2-SKP2-SIRT3 (association, anti bait coimmunoprecipitation) Inuzuka et al., Cell 2012
• IRef Intact Interaction: Complex of 18 proteins (association, tandem affinity purification) Varjosalo et al., Cell reports 2013
• IRef Intact Interaction: Complex of 30 proteins (association, tandem affinity purification) Varjosalo et al., Nat Methods 2013
• IRef Intact Interaction: Complex of CDK2-RBX1-CDKN1B-SKP1-SKP2-CKS1B-CCNA2-CUL1 (association, molecular sieving) Hao et al., Mol Cell 2005
• IRef Intact Interaction: Complex of SKP2-CCNA1-CDK2-CCNA2-CDK1-CDT1 (association, coimmunoprecipitation) Sugimoto et al., J Biol Chem 2004
• IRef Ophid Interaction: SKP2 — CDK2 (aggregation, confirmational text mining) Bilodeau et al., FEBS Lett 1999*
• IRef Ophid Interaction: SKP2 — CDK2 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Sugimoto et al., J Biol Chem 2004 : Cdk phosphorylation resulted in the binding of Cdt1 to the F-box protein Skp2 and subsequent degradation
Li et al., J Biol Chem 2004 (Ovarian Neoplasms) : It is the combined effect of 1,25 ( OH ) ( 2 ) D ( 3 ) on both the CDK2 dependent phosphorylation of p27, and thus its affinity for Skp2, and Skp2 expression that dramatically increases the stability of the p27 protein
Takeda et al., J Biol Chem 2005 : Using phosphopeptide mapping and mutagenesis studies, we found that threonine 29 within the N terminus of Cdt1 is phosphorylated by Cdk2 and required for interaction with Skp2
Shin et al., Int J Oncol 2008 (Ovarian Neoplasms) : Therefore, these results suggest that serum starvation induces G1 arrest through suppression of Skp2 dependent CDK2 activity and Skp2 independent CDK4 activity in human SK-OV-3 ovarian cancer cells
Qiao et al., J Biol Chem 2012 : Specifically, GPC1 suppressed CDK inhibitors (CKIs) , including p21, p27, p16, and p19, and the D cyclins, and induced CDK2 and Skp2
Yam et al., Mol Cell Biol 1999 : We found that Skp2 can inhibit the kinase activity of cyclin A-Cdk2 in vitro, both by direct inhibition of cyclin A-Cdk2 and by inhibition of the activation of Cdk2 by cyclin dependent kinase (CDK) activating kinase phosphorylation ... Only the kinase activity of Cdk2 , not of that of Cdc2 or Cdk5, is reduced by Skp2 ... Skp2 is phosphorylated by cyclin A-Cdk2 on residue Ser76, but nonphosphorylatable mutants of Skp2 can still inhibit the kinase activity of cyclin A-Cdk2 toward histone H1