Cooperation of a single lysine mutation and a C-terminal domain in the cytoplasmic sequestration of the p53 protein.
TLDR
Results indicated the involvement of cis-acting sequences in the regulation of p53 subcellular localization in human MCF-7 breast cancer, RKO colon cancer, and SAOS-2 sarcoma cells.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-07-31 and is currently open access. It has received 52 citations till now. The article focuses on the topics: Nuclear protein & Protein subcellular localization prediction.read more
Citations
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Journal ArticleDOI
A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking.
Jayne M. Stommel,Natalie D. Marchenko,Gretchen S. Jimenez,Ute M. Moll,Thomas J. Hope,Geoffrey M. Wahl +5 more
TL;DR: A model in which regulated p53 tetramerization occludes its NES is proposed, thereby ensuring nuclear retention of the DNA‐binding form and suggesting that attenuation of p53 function involves the conversion of tetramers into monomers or dimers, in which the NES is exposed to the proteins which mediate their export to the cytoplasm.
Journal ArticleDOI
Nuclear transport and cancer: from mechanism to intervention.
TL;DR: This work has shown that disruption of nuclear-cytoplasmic transport promote transformation, and is this process a viable therapeutic target?
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Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
TL;DR: It is suggested that p53 C-terminal lysine residues are the main sites of ubiquitin ligation, which target p53 for proteasome-mediated degradation.
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A chemical genetic screen identifies inhibitors of regulated nuclear export of a Forkhead transcription factor in PTEN-deficient tumor cells.
Tweeny R Kau,Frank C. Schroeder,Shivapriya Ramaswamy,Cheryl L Wojciechowski,Jean J. Zhao,Thomas M. Roberts,Jon Clardy,William R. Sellers,Pamela A. Silver +8 more
TL;DR: Novel general export inhibitors were found that react with CRM1 as well as a number of compounds that inhibit PI3K/Akt signaling, among which are included multiple antagonists of calmodulin signaling.
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Parc: A Cytoplasmic Anchor for p53
TL;DR: The identification of Parc, a Parkin-like ubiquitin ligase, as a cytoplasmic anchor protein in p53-associated protein complexes reveals that Parc is a critical regulator in controlling p53 subcellular localization and subsequent function.
References
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WAF1, a potential mediator of p53 tumor suppression
Wafik S. El-Deiry,Takashi Tokino,Victor E. Velculescu,Daniel B. Levy,Ramon Parsons,Jeffrey M. Trent,D Lin,W. Edward Mercer,Kenneth W. Kinzler,Bert Vogelstein +9 more
TL;DR: A gene is identified, named WAF1, whose induction was associated with wild-type but not mutant p53 gene expression in a human brain tumor cell line and that could be an important mediator of p53-dependent tumor growth suppression.
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p53 mutations in human cancers
TL;DR: The p53 mutational spectrum differs among cancers of the colon, lung, esophagus, breast, liver, brain, reticuloendothelial tissues, and hemopoietic tissues as mentioned in this paper.
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p53, the Cellular Gatekeeper for Growth and Division
TL;DR: The author regrets the lack of citations for many important observations mentioned in the text, but their omission is made necessary by restrictions in the preparation of review manuscripts.
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Green fluorescent protein as a marker for gene expression
TL;DR: A complementary DNA for the Aequorea victoria green fluorescent protein produces a fluorescent product when expressed in prokaryotic or eukaryotic cells, which can be used to monitor gene expression and protein localization in living organisms.
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Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
T Miyashita,John C. Reed +1 more
TL;DR: The bax gene promoter region contains four motifs with homology to consensus p53-binding sites and wild-type but not mutant p53 protein bound to oligonucleotides corresponding to this region of the bax promoter, suggesting that bax is a p53 primary-response gene, presumably involved in a p 53-regulated pathway for induction of apoptosis.