Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover (Q24336311)

GOA release 2020-03-11

author name string

Sylvia S Dias

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Carol Hogan

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Anna-Maria Ochocka

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David W Meek

Coping with stress: multiple ways to activate p53.

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language of work or name

English

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publication date

19 November 2009

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published in

FEBS Letters

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volume

583

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issue

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page(s)

3543-8

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cites work

1 reference

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Inhibition of Polo-like kinase-1 by DNA damage occurs in an ATM- or ATR-dependent fashion.

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Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover

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Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance

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Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2.

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Transcription factor TAFII250 promotes Mdm2-dependent turnover of p53

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A novel site of AKT-mediated phosphorylation in the human MDM2 onco-protein

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Elevated levels of oncogenic protein kinase Pim-1 induce the p53 pathway in cultured cells and correlate with increased Mdm2 in mantle cell lymphoma.

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p53 isoforms can regulate p53 transcriptional activity.

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Phage-peptide display identifies the interferon-responsive, death-activated protein kinase family as a novel modifier of MDM2 and p21WAF1.

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Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation

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Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate.

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p53 stabilization in response to DNA damage requires Akt/PKB and DNA-PK.

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Polo-like kinase-1 is a target of the DNA damage checkpoint

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Dual-site regulation of MDM2 E3-ubiquitin ligase activity

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