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MDM2 — MTBP
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
MTBP
—
MDM2
(direct interaction, pull down)
Boyd et al., J Biol Chem 2000*
-
IRef Biogrid Interaction:
MTBP
—
MDM2
(physical association, affinity chromatography technology)
Boyd et al., J Biol Chem 2000*
-
IRef Biogrid Interaction:
MTBP
—
MDM2
(direct interaction, two hybrid)
Boyd et al., J Biol Chem 2000*
-
IRef Biogrid Interaction:
MTBP
—
MDM2
(physical association, affinity chromatography technology)
Brady et al., Mol Cell Biol 2005*
-
IRef Hprd Interaction:
MTBP
—
MDM2
(in vitro)
Boyd et al., J Biol Chem 2000*
-
IRef Hprd Interaction:
Complex of 36 proteins
(in vivo)
Maguire et al., Cancer Res 2008
-
IRef Hprd Interaction:
Complex of MDM4-MDM2-DHFR-MTBP-PSMD10-RB1
(in vivo)
Maguire et al., Cancer Res 2008
Text-mined interactions from Literome
Brady et al., Mol Cell Biol 2005
:
Regulation of p53 and
MDM2 activity by
MTBP ... Our findings suggest that
MTBP differentially
regulates the E3 ubiquitin ligase activity of
MDM2 towards two of its most critical targets ( itself and p53 ) and in doing so significantly contributes to MDM2 dependent p53 homeostasis in unstressed cells
Odvody et al., Oncogene 2010
(Lymphoma, B-Cell) :
Surprisingly, reduced levels of
Mtbp did not lead to an increase in B-cell apoptosis or
affect Mdm2