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EIF4E — PML
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
EIF4E
—
PML
(colocalization, imaging technique)
Topisirovic et al., Mol Cell Biol 2002*
-
IRef Biogrid Interaction:
EIF4E
—
PML
(direct interaction, pull down)
Cohen et al., EMBO J 2001*
-
IRef Biogrid Interaction:
EIF4E
—
PML
(direct interaction, pull down)
Kentsis et al., J Mol Biol 2001*
-
IRef Hprd Interaction:
EIF4E
—
PML
(in vitro)
Cohen et al., EMBO J 2001*
-
IRef Intact Interaction:
Complex of NXF1-PML-EIF4E
(association, anti bait coimmunoprecipitation)
Topisirovic et al., EMBO J 2009
-
IRef Ophid Interaction:
EIF4E
—
PML
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
-
IRef Ophid Interaction:
EIF4E
—
PML
(aggregation, confirmational text mining)
Cohen et al., EMBO J 2001*
Text-mined interactions from Literome
Cohen et al., EMBO J 2001
(Cell Transformation, Neoplastic...) :
Additionally,
PML reduces the affinity of
eIF4E for m ( 7 ) G mRNA cap, causing a reduction in Cyclin D1 protein levels and consequent transformation inhibition
Kentsis et al., J Mol Biol 2001
:
PML and Z profoundly
reduce the affinity of
eIF4E for its substrate, the 5 ' 7-methyl guanosine cap of mRNA, by over 100-fold
Volpon et al., Proc Natl Acad Sci U S A 2010
:
Our results provide a molecular basis for how
PML and Z RINGs
reduce the affinity of
eIF4E for the m ( 7 ) G cap and thereby act as key inhibitors of eIF4E function