Detail information of PPI "HPI103503"

Interactionp53  <==>  MDM2
Role & StateRS:0000002,activity; RS:0000001,posttranslational modification; RS:0000074,inhibitor;
Interaction TypeIT:0000130,overexpression; IT:0000073,attachment; IT:0000262,react; IT:0000227,bind; IT:0000078,regulation; IT:0000092,degradation; IT:0000168,inhibit; IT:0000082,influence; IT:0000123,ubiquitination; IT:0000114,activation; IT:0000099,formation; IT:0000085,synthesis; IT:0000076,inhibition;
Biological ProcessBP:0032774,RNA synthesis; BP:0006915,apoptosis; BP:0006412,protein synthesis; BP:0016446,mutation; BP:0006412,translation;
Biological FunctionBF:0016874,ligase activity;
Subcelluar LocationSCL:0000016,ribosome;
Detection Method        ---
Reference12536604_0, [Role of functional inactivation of p53 from MDM2 overexpression in hepatocarcinogenesis].
Reference16201274_6, It was suggested that in the HepG2 cells, SUMO-1 can increase the apoptosis induced by wild-type p53 through binding to p53 protein, posttranslational modification and inhibiting the p53 degradation by MDM2.
Reference17363365_7, Finally, ubiquitinated p53 accumulated in a pAb-240 reactive form when p53 degradation was blocked by proteasome inhibition, and a p53-ubiquitin fusion protein displayed a mutant-only conformation in MDM2-null cells.
Reference17363365_9, The covalent attachment of ubiquitin may lock p53 in a mutant conformation in the absence of MDM2-binding and prior to its degradation by the proteasome.
Reference20019189_5, Iron status influenced p53 ubiquitination and degradation rate, and the MDM2 inhibitor nutlin increased p53 levels in iron-depleted cells.
Reference20019189_7, The MDM2 -309T G promoter polymorphism, determining increased MDM2 and lower p53 activity, was associated with higher risk of hepatocarcinoma in cirrhotic patients with hemochromatosis, and with HFE mutations in patients with hepatocarcinoma without hemochromatosis, suggesting an interaction between MDM2 and iron in the pathogenesis of hepatocarcinoma.
Reference20019189_8, In conclusion, iron status influences p53 activity and antioxidant response by modulating MDM2 expression.
Reference20849854_0, Overexpression of SCYL1-BP1 stabilizes functional p53 by suppressing MDM2-mediated ubiquitination.
Reference21060154_4, We found that Enigma elicited p53 degradation by inhibiting MDM2 self-ubiquitination and increasing its ubiquitin ligase activity toward p53 in cells.
Reference21399665_4, We found that a downregulation of rRNA synthesis, induced by silencing the POLR1A gene coding for the RNA polymerase I catalytic subunit, stabilised p53 without altering the nucleolar integrity in human cancer cells. p53 stabilisation was due to the inactivation of the MDM2-mediated p53 degradation by the binding of ribosomal proteins no longer used for ribosome building. p53 stabilisation did not occur when rRNA synthesis downregulation was associated with a contemporary reduction of protein synthesis.