MDM2p53

MDM2p53 refers to the interaction between two key proteins involved in cell cycle regulation and tumor suppression: MDM2 and p53. MDM2, also known as double minute 2 homolog, is a ubiquitin ligase. Its primary function in this context is to regulate the stability and activity of the p53 protein. p53 is a tumor suppressor protein that plays a critical role in preventing the development of cancer. It is activated in response to various cellular stresses, such as DNA damage or oncogene activation.

Once activated, p53 can induce cell cycle arrest, DNA repair, or apoptosis (programmed cell death), thereby eliminating damaged cells. MDM2 acts as a negative regulator of p53. It binds to p53 and targets it for ubiquitination, a process that leads to p53 degradation by the proteasome. This interaction is crucial for maintaining a low basal level of p53 in unstressed cells.

Under conditions of cellular stress, the MDM2-p53 interaction is often disrupted. This can occur through various mechanisms, leading to an accumulation and activation of p53. The MDM2-p53 feedback loop is a tightly controlled system. Dysregulation of this interaction, often through overexpression of MDM2, can lead to the inactivation of p53 and contribute to tumor formation. Therefore, the MDM2-p53 axis is a significant target in cancer research and therapy.