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Molecular and Biochemical Techniques for Deciphering p53-MDM2 Regulatory Mechanisms
- Source :
- Biomolecules, COLIBRI, Universidad de la República, instacron:Universidad de la República, Biomolecules, Vol 11, Iss 36, p 36 (2021)
- Publication Year :
- 2020
-
Abstract
- The p53 and Mouse double minute 2 (MDM2) proteins are hubs in extensive networks of interactions with multiple partners and functions. Intrinsically disordered regions help to adopt function-specific structural conformations in response to ligand binding and post-translational modifications. Different techniques have been used to dissect interactions of the p53-MDM2 pathway, in vitro, in vivo, and in situ each having its own advantages and disadvantages. This review uses the p53-MDM2 to show how different techniques can be employed, illustrating how a combination of in vitro and in vivo techniques is highly recommended to study the spatio-temporal location and dynamics of interactions, and to address their regulation mechanisms and functions. By using well-established techniques in combination with more recent advances, it is possible to rapidly decipher complex mechanisms, such as the p53 regulatory pathway, and to demonstrate how protein and nucleotide ligands in combination with post-translational modifications, result in inter-allosteric and intra-allosteric interactions that govern the activity of the protein complexes and their specific roles in oncogenesis. This promotes elegant therapeutic strategies that exploit protein dynamics to target specific interactions.
- Subjects :
- 0301 basic medicine
p53
MDMX
Multiple Partners
lcsh:QR1-502
protein-protein interactions
p53 mRNA
Cell Cycle Proteins
Computational biology
Review
DNA damage response
Biochemistry
P53 mdm2
lcsh:Microbiology
Protein–protein interaction
03 medical and health sciences
Mice
0302 clinical medicine
MDM2
Animals
Humans
Phosphorylation
Molecular Biology
protein-RNA interactions
biology
Chemistry
Protein dynamics
Biochemistry and Molecular Biology
Nuclear Proteins
Proto-Oncogene Proteins c-mdm2
030104 developmental biology
post-translational modification
030220 oncology & carcinogenesis
ATM
biology.protein
Posttranslational modification
Mdm2
Regulatory Pathway
Tumor Suppressor Protein p53
Protein Processing, Post-Translational
Biokemi och molekylärbiologi
DNA Damage
Protein Binding
Subjects
Details
- ISSN :
- 2218273X
- Volume :
- 11
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biomolecules
- Accession number :
- edsair.doi.dedup.....f8e23b210e4fcc1a369f07413b95d3c7