p53 Suppresses E2F1-dependent PLK1 expression upon DNA damage by forming p53–E2F1–DNA complex

Zhou, Zhe; Chen, Jixiang; Li, Shuyan; An, Guo-Shun; Ni, Jing; Jia, Hong-Ti

doi:10.1016/j.yexcr.2013.09.012

Cited by 27 publications

(24 citation statements)

References 46 publications

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“…39 We recently showed that DNA damage increased the interaction between p53 and E2F1 in the nuclei, leading to repression of E2F1-dependent PLK1 gene by p53. 40 Therefore, the early nucleolar accumulation of E2F1 might be advantageous to the function of p53 in the nucleoplasm, induce cell cycle arrest or apoptosis, thereby maintaining genomic stability. Together, the early nucleolar accumulation of E2F1 may function as a buffer to produce a cushioning effect on the responsive elevation of E2F1 in the early response to DNA damage, which coordinates the diversifying mechanisms of E2F1 acts in controlling cell death/survival, cell cycle arrest, and DNA repair in the acute response to DNA damage.…”

Section: Discussionmentioning

confidence: 99%

ATM-dependent E2F1 accumulation in the nucleolus is an indicator of ribosomal stress in early response to DNA damage

Jin

et al. 2014

Cell Cycle

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Section: Discussionmentioning

confidence: 99%

ATM-dependent E2F1 accumulation in the nucleolus is an indicator of ribosomal stress in early response to DNA damage

Jin

et al. 2014

Cell Cycle

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“…The roles of p53 inducing cell cycle arrest rivals with Plk1 functions which promotes the progression of the cell cycle. Plk1 is inhibitied by ATM/ATR dependent fashion after DNA damage (11,44), and is transcriptionally regulated either directly or indirectly by p53 (62-64). It localizes to the Plk1 promoter and binds to E2F1 which induces an increment of transcriptional level of Plk1.…”

Section: Relationship Between Plk1 and P53 In Dna Damage Responsementioning

confidence: 99%

“…It localizes to the Plk1 promoter and binds to E2F1 which induces an increment of transcriptional level of Plk1. Its binding forms p53-E2F1-Plk1 promoter DNA complex and suppresses the expression of Plk1 (62). Furthermore, the expression of Plk1 is indirectly repressed by p53 through either targeting a sequence of CDE/CHR within Plk1 promoter by p21/waf1 or a negative regulation of FoxM1 (forhead box M1), which stimulates Plk1 expression caused by p53 (63,64).…”

Section: Relationship Between Plk1 and P53 In Dna Damage Responsementioning

confidence: 99%

Polo-like kinase-1 in DNA damage response

Hyun¹,

Hwan²,

Jang³

2014

BMB Reports

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Polo-like kinase-1 (Plk1) belongs to a family of serine-threonine kinases and plays a critical role in mitotic progression. Plk1 involves in the initiation of mitosis, centrosome maturation, bipolar spindle formation, and cytokinesis, well-reported as traditional functions of Plk1. In this review, we discuss the role of Plk1 during DNA damage response beyond the functions in mitotsis. When DNA is damaged in cells under various stress conditions, the checkpoint mechanism is activated to allow cells to have enough time for repair. When damage is repaired, cells progress continuously their division, which is called checkpoint recovery. If damage is too severe to repair, cells undergo apoptotic pathway. If damage is not completely repaired, cells undergo a process called checkpoint adaptation, and resume cell division cycle with damaged DNA. Plk1 targets and regulates many key factors in the process of damage response, and we deal with these subjects in this review. [BMB Reports 2014; 47(5): 249-255]

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“…If the DNA damage response is triggered during S/G2 interphase, cell division is halted by G2 DNA damage checkpoint and PLK1 remains inactive. Activated ATM/ATR phosphorylates Bora at threonine 501 residue, resulting in degradation of Bora by E3 ubiquitin ligase SCF-b-TRCP 14. PLK1 cannot be phosphorylated by Aurora A without the facilitation of Bora, leading to inhibition of Cdc25 phosphatase, which in turn deactivates CDK1 that signals the mitotic entry.…”

Section: Introductionmentioning

confidence: 99%

“…On the other hand, p53 regulates the transcription of PLK1 as well as other mitotic regulators such as cyclin A and cyclin B. Stabilised p53 is localised to the promoter region of PLK1, binding to E2F and thus preventing E2F from promoting the transcription of PLK1 by forming p53–E2F–PLK1 promoter complex 14. In addition, p53 also activates p21/Waf1 that binds to the promoter region of PLK1 and inhibits PLK1 at the transcriptional level.…”

Section: Introductionmentioning

confidence: 99%

Molecular interactions of polo-like kinase 1 in human cancers

et al. 2016

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Polo-like kinase 1 (PLK1) is an essential protein in communicating cell-cycle progression and DNA damage. Overexpression of PLK1 has been validated as a marker for poor prognosis in many cancers. PLK1 knockdown decreases the survival of cancer cells. PLK1 is therefore an attractive target for anticancer treatments. Several inhibitors have been developed, and some have been clinically tested to show additive effects with conventional therapies. Upstream regulation of PLK1 involves multiple interactions of proteins such as FoxM1, E2F and p21. Other cancer-related proteins such as pRB and p53 also indirectly influence PLK1 expression. With the high mutation rates of these genes seen in cancers, they may be associated with PLK1 deregulation. This raises the question of whether PLK1 overexpression is a cause or a consequence of oncogenesis. In addition, hypomethylation of the CpG island of the PLK1 promoter region contributes to its upregulation. PLK1 expression can be affected by many factors; thus, it is possible that PLK1 deregulation in each individual patient tumours could be due to different underlying mechanisms.

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p53 Suppresses E2F1-dependent PLK1 expression upon DNA damage by forming p53–E2F1–DNA complex

Cited by 27 publications

References 46 publications

ATM-dependent E2F1 accumulation in the nucleolus is an indicator of ribosomal stress in early response to DNA damage

ATM-dependent E2F1 accumulation in the nucleolus is an indicator of ribosomal stress in early response to DNA damage

Polo-like kinase-1 in DNA damage response

Molecular interactions of polo-like kinase 1 in human cancers

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