◀ Back to CDK2
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