The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
p53 Isoforms: Key Regulators of the Cell Fate Decision
Open accessAbstract
It is poorly understood how a single protein, p53, can be responsive to so many stress signals and orchestrates very diverse cell responses to maintain/restore cell/tissue functions. The uncovering that TP53 gene physiologically expresses, in a tissue-dependent manner, several p53 splice variants (isoforms) provides an explanation to its pleiotropic biological activities. Here, we summarize a decade of research on p53 isoforms. The clinical studies and the diverse cellular and animal models of p53 isoforms (zebrafish, Drosophila, and mouse) lead us to realize that a p53-mediated cell response is, in fact, the sum of the intrinsic activities of the coexpressed p53 isoforms and that unbalancing expression of different p53 isoforms leads to cancer, premature aging, (neuro)degenerative diseases, inflammation, embryo malformations, or defects in tissue regeneration. Cracking the p53 isoforms' code is, thus, a necessary step to improve cancer treatment. It also opens new exciting perspectives in tissue regeneration.
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Cites
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551 · cited 1×
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Mutant p53 gain of function in two mouse models of Li-Fraumeni syndrome
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p53 isoforms can regulate p53 transcriptional activity
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Self-citationp53 isoforms Δ133p53 and p53β are endogenous regulators of replicative cellular senescence
Fujita, K., Mondal, A. M., Horikawa, I., Nguyen, G. H., Kumamoto, K., Sohn, J. J., Bowman, E. D., Mathe, E. A., Schetter, A. J., Pine, S. R., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1928 · Cited by 336
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p53 isoforms regulate aging- and tumor-associated replicative senescence in T lymphocytes
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p53 ancestry: gazing through an evolutionary lens
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Detecting p53 Isoforms at Protein Level
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Self-citation
Cited by
Chen, J., Crutchley, J., Zhang, D., Owzar, K., & Kastan, M. B. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0908 · Cited by 93
Structural Evolution and Dynamics of the p53 Proteins
Chillemi, G., Kehrloesser, S., Bernassola, F., Desideri, A., Dötsch, V., Levine, A. J., & Melino, G. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a028308 · Cited by 65
TP53 Mutation in Acute Myeloid Leukemia: An Old Foe Revisited
Shin, D.-Y. (2023) · Cancers · doi:10.3390/cancers15194816 · Cited by 46
Nutrigenomics at the Interface of Aging, Lifespan, and Cancer Prevention
Riscuta, G. (2016) · The Journal of Nutrition · doi:10.3945/jn.116.235119 · Cited by 37
Metadata
- Authors
- Joruiz, S. M., & Bourdon, J.-C.
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2016-01-22
- Volume
- 6
- Issue
- 8
- Pages
- a026039
- ISSN
- 2157-1422 (ISSN-L)
- OpenAlex
- W2264082883
- Cited by
- 190
- References
- 10
- Type
- posted content
- Language
- en
- Open access
- bronze
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