PP2A-PP2R5C dephosphorylates MDM2

Stable Identifier
R-HSA-6792863
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

The protein serine/threonine phosphatase complex PP2A, recruited to MDM2 through interaction of the PP2A regulatory subunit PPP2R5C and cyclin G1 (CCNG1) dephosphorylates MDM2 on threonine residue T218 (T218 in human MDM2 corresponds to T216 in mouse Mdm2). Dephosphorylation of T218 increases the affinity of MDM2 for TP53 (p53), leading to p53 down-regulation (Okamoto et al. 2002).

CCNG1-recruited PP2A can also dephosphorylate serine residue S166 of human MDM2 (Okamoto et al. 2002).

Literature References
PubMed ID Title Journal Year
11983168 Cyclin G recruits PP2A to dephosphorylate Mdm2 Mol. Cell 2002
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein serine/threonine phosphatase activity of PPP2A-PPPR5C:CCNG1:(p-T218-MDM2, p-S166-MDM2) [nucleoplasm]
Physical Entity
Activity
Orthologous Events