A new function for p53 tetramerization domain in cell fate control

Zhang, Jin; Lucchesi, Christopher A.; Chen, Xinbin

doi:10.1080/15384101.2016.1204868

Cited by 4 publications

(3 citation statements)

References 7 publications

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“…Each labeled gray bubble represents proteins that serve as binding partners at their purported domains. [12][13][14][15][16][17][18][19] B, Multiple conformations (i-iii) sampled by p53 with transient helices persisting detected through various NMR experiments. Upon associating with MDM2, the trans-activation domain located within the N-terminal domain (lavender), the helical structure is stabilized [13,20,21] 3 | THE ASSEMBLY PATHWAY With nucleation energetics regulating structural specificity, understanding the entire peptide assembly pathway may lead to regulation strategies for the templated information.…”

Section: Energetic Contributions Regulating Cross-β Assemblymentioning

confidence: 99%

“…Each labeled gray bubble represents proteins that serve as binding partners at their purported domains. [ 12–19 ] B, Multiple conformations (i–iii) sampled by p53 with transient helices persisting detected through various NMR experiments. Upon associating with MDM2, the trans‐activation domain located within the N‐terminal domain (lavender), the helical structure is stabilized [ 13,20,21 ]…”

Section: Introductionmentioning

confidence: 99%

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Capturing nested information from disordered peptide phases

2020

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Anfinsen's dogma emerged from experiments which show that a protein's native 3D folded architecture is encoded within its primary sequence. This insight emerged before almost 40% of eukaryotic proteins were found to contain intrinsically disordered domains with binding partners that are able to template multiple structures and functional outputs. Despite the challenges associated with characterizing such intrinsically disordered protein domains and their interactions with various binding partners, the need to understand how they propagate and regulate context-dependent information now becomes increasingly important. In addition to understanding the complex signaling networks of multicellular organisms, harness their potential will expand the next generation of functional materials. Accordingly, we review progress with model peptides to reveal the rules necessary for precise spatiotemporal assembly of polypeptide materials.

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Section: Energetic Contributions Regulating Cross-β Assemblymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Capturing nested information from disordered peptide phases

2020

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“…В системе in vitro, на клеточной линии H1299 (карцинома лёгкого, ноль-мутант по р53) показано, что инактивация тетрамера белка р53, то есть потеря транскрипционной активности достигается в случае мутаций трёх субъединиц (R249S, R273H), дефектных по связыванию с ДНК и одной укороченной субъединицы р53, лишённой N-концевого трансактивационного домена [92]. В мономерном состоянии белок р53 не способен к активации генов [93]. Следует отметить, что ПТМ подвергается как p53, так и гистоны вблизи от его мест связывания в хроматине, что даёт возможность осуществлять совместную трансактивацию генов-мишеней с высокой точностью [10,17,89].…”

Section: белок р53 как транскрипционный факторunclassified

Structural-functional diversity of p53 proteoforms

Naryzhny

Legina

2019

BIOMED KHIM

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Protein p53 is one of the most studied proteins. This attention is primarily due to its key role in the cellular mechanisms associated with carcinogenesis. Protein p53 is a transcription factor involved in a wide variety of processes: cell cycle regulation and apoptosis, signaling inside the cell, DNA repair, coordination of metabolic processes, regulation of cell interactions, etc. This multifunctionality is apparently determined by the fact that p53 is a vivid example of how the same protein can be represented by numerous proteoforms bearing completely different functional loads. By alternative splicing, using different promoters and translation initiation sites, the TP53 gene gives rise to at least 12 isoforms, which can additionally undergo numerous (>200) post-translational modifications. Proteoforms generated due to numerous point mutations in the TP53 gene are adding more complexity to this picture. The proteoforms produced are involved in various processes, such as the regulation of p53 transcriptional activity in response to various factors. This review is devoted to the description of the currently known p53 proteoforms, as well as their possible functionality.

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GINS4 suppresses ferroptosis by antagonizing p53 acetylation with Snail

Chen

Cai

Yang

et al. 2023

Proc. Natl. Acad. Sci. U.S.A.

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Ferroptosis is an iron-dependent oxidative, nonapoptotic form of regulated cell death caused by the destruction of redox homeostasis. Recent studies have uncovered complex cellular networks that regulate ferroptosis. GINS4 is a promoter of eukaryotic G 1 /S - cell cycle as a regulator of initiation and elongation of DNA replication, but little is known about its impact on ferroptosis. Here, we found that GINS4 was involved in the regulation of ferroptosis in lung adenocarcinoma (LUAD). CRISPR/Cas9-mediated GINS4 KO facilitated ferroptosis. Interestingly, depletion of GINS4 could effectively induce G1, G 1 /S, S, and G 2 /M cells to ferroptosis, especially for G2/M cells. Mechanistically, GINS4 suppressed p53 stability through activating Snail that antagonized the acetylation of p53, and p53 lysine residue 351 (K351 for human p53) was the key site for GINS4-suppressed p53-mediated ferroptosis. Together, our data demonstrate that GINS4 is a potential oncogene in LUAD that functions to destabilize p53 and then inhibits ferroptosis, providing a potential therapeutic target for LUAD.

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A new function for p53 tetramerization domain in cell fate control

Cited by 4 publications

References 7 publications

Capturing nested information from disordered peptide phases

Capturing nested information from disordered peptide phases

Structural-functional diversity of p53 proteoforms

GINS4 suppresses ferroptosis by antagonizing p53 acetylation with Snail

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