PIDD1: A Potential Drug Target and Biomarker for p53-Induced Cell Death

Target Name: PIDD1

NCBI ID: G55367

PIDD1

PIDD1: A Potential Drug Target and Biomarker for p53-Induced Cell Death

p53 is a well-known tumor suppressor gene that plays a crucial role in regulating cell growth and apoptosis. p53 mutations have been implicated in numerous diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. The discovery of novel targets for p53 regulation has the potential to lead to new therapeutic approaches for these diseases. One such target is PIDD1 (p53-induced death domain-containing protein 1), a protein that has been shown to interact with p53 and may play a role in regulating p53-mediated cell death. In this article, we will explore the biology of PIDD1 and its potential as a drug target and biomarker.

Overview of PIDD1

PIDD1 is a 14-kDa protein that is expressed in various tissues and cell types, including muscle, nerve, and heart cells. PIDD1 was identified as a gene that was co-expressed with p53 in various tissues and was shown to interact with p53 in a cell-surface dependent manner. This interaction between PIDD1 and p53 led to the formation of a complex that was characterized by increased p53 stability and the formation of a Death Domain (DDP) in the p53 protein.

The PIDD1-p53 complex plays a role in regulating cell death, which is a critical process in various biological processes, including development, growth, and maintenance of tissue homeostasis. p53 is known for its ability to induce apoptosis, which is a programmed cell death that is regulated by various factors, including p53 itself. The PIDD1-p53 complex may be involved in the regulation of p53-mediated cell death by affecting the stability and function of p53.

PIDD1 as a drug target

The potential of PIDD1 as a drug target is based on its interaction with p53 and its ability to regulate p53-mediated cell death. Several studies have shown that inhibition of PIDD1 can lead to increased p53 stability and the formation of the Death Domain in p53, which can lead to the inhibition of p53-mediated cell death. This suggests that PIDD1 may be a useful target for therapies that are aimed at increasing the efficacy of p53-mediated cell death.

One of the potential mechanisms by which PIDD1 may be targeted by drugs is through its role in the regulation of p53 stability. Activated p53 can form a Death Domain, which is a region of p53 that is known to enhance the stability of p53 and increase its resistance to ubiquitination and degradation. By inhibiting PIDD1, drugs may be able to reduce the formation of the Death Domain and increase the stability of p53, leading to the inhibition of p53-mediated cell death.

Another potential mechanism by which PIDD1 may be targeted by drugs is through its role in the regulation of p53-mediated cell death. PIDD1 has been shown to interact with p53 and may play a role in regulating the stability and function of p53. By inhibiting PIDD1, drugs may be able to reduce the inhibition of p53-mediated cell death that is caused by the formation of the Death Domain in p53.

PIDD1 as a biomarker

PIDD1 may also be used as a biomarker for the detection and monitoring of p53-mediated cell death. The formation of the Death Domain in p53 can be detected using various techniques, including immunofluorescence and Western blotting. By detecting the formation of the Death Domain in p53, researchers can monitor the level of p53-mediated cell death and assess the efficacy of therapies that are aimed at increasing the efficacy of p53-mediated cell death.

In addition to its potential as a drug target, PIDD1 may also be used as a biomarker for

Protein Name: P53-induced Death Domain Protein 1

Functions: Component of the DNA damage/stress response pathway that functions downstream of p53/TP53 and can either promote cell survival or apoptosis (PubMed:10973264, PubMed:15073321, PubMed:16360037, PubMed:17159900). Associated with CRADD and the CASP2 caspase, it forms the PIDDosome a complex that activates CASP2 and triggers apoptosis (PubMed:15073321, PubMed:17159900). Associated with IKBKG and RIPK1, it enhances sumoylation and ubiquitination of IKBKG which is important for activation of the transcription factor NF-kappa-B (PubMed:16360037, PubMed:17159900)

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