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

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Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover. / Dias, Sylvia S.; Hogan, Carol; Ochocka, Anna Maria; Meek, David W.

In: FEBS Letters, Vol. 583, No. 22, 19.11.2009, p. 3543-3548.

Research output: Contribution to journalArticle

Harvard

Dias, SS, Hogan, C, Ochocka, AM & Meek, DW 2009, 'Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover' FEBS Letters, vol 583, no. 22, pp. 3543-3548., 10.1016/j.febslet.2009.09.057

APA

Dias, S. S., Hogan, C., Ochocka, A. M., & Meek, D. W. (2009). Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover. FEBS Letters, 583(22), 3543-3548. 10.1016/j.febslet.2009.09.057

Vancouver

Dias SS, Hogan C, Ochocka AM, Meek DW. Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover. FEBS Letters. 2009 Nov 19;583(22):3543-3548. Available from: 10.1016/j.febslet.2009.09.057

Author

Dias, Sylvia S.; Hogan, Carol; Ochocka, Anna Maria; Meek, David W. / Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover.

In: FEBS Letters, Vol. 583, No. 22, 19.11.2009, p. 3543-3548.

Research output: Contribution to journalArticle

Bibtex - Download

@article{bbeff033048645dba02d9720f5251dde,
title = "Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover",
keywords = "p53, Murne double-minute clone 2, Polo-like kinase-1, Phosphorylation, CULTURED-CELLS, PROTEIN, HDM2, BINDING, DOMAIN, PLK1, SITE, STABILITY, PATHWAY",
author = "Dias, {Sylvia S.} and Carol Hogan and Ochocka, {Anna Maria} and Meek, {David W.}",
year = "2009",
doi = "10.1016/j.febslet.2009.09.057",
volume = "583",
number = "22",
pages = "3543--3548",
journal = "FEBS Letters",
issn = "0014-5793",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Polo-like kinase-1 phosphorylates MDM2 at Ser260 and stimulates MDM2-mediated p53 turnover

A1 - Dias,Sylvia S.

A1 - Hogan,Carol

A1 - Ochocka,Anna Maria

A1 - Meek,David W.

AU - Dias,Sylvia S.

AU - Hogan,Carol

AU - Ochocka,Anna Maria

AU - Meek,David W.

PY - 2009/11/19

Y1 - 2009/11/19

N2 - <p>The E3 ubiqutin ligase, murne double-minute clone 2 (MDM2), promotes the degradation of p53 under normal homeostatic conditions. Several serine residues within the acidic domain of MDM2 are phosphorylated to maintain its activity but become hypo-phosphorylated following DNA damage, leading to inactivation of MDM2 and induction of p53. However, the signalling pathways that mediate these phosphorylation events are not fully understood. Here we show that the oncogenic and cell cycle-regulatory protein kinase, polo-like kinase-1 (PLK1), phosphorylates MDM2 at one of these residues, Ser260, and stimulates MDM2-mediated turnover of p53. These data are consistent with the idea that deregulation of PLK1 during tumourigenesis may help suppress p53 function.</p><p>Structured summary:</p><p>MINT-7266353: MDM2 (uniprotkb:Q00987) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by pull down (MI:0096)</p><p>MINT-7266344, MINT-7266329: MDM2 (uniprotkb:Q00987) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by anti bait coimmunoprecipitation (MI:0006)</p><p>MINT-7266250: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) p53 (uniprotkb:P04637) by protein kinase assay (MI:0424)</p><p>MINT-7266241, MINT-7266318: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) MDM2 (uniprotkb:P23804) by protein kinase assay (MI:0424)</p><p>MINT-7266231, MINT-7266805, MINT-7266264, MINT-7266299: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) MDM2 (uniprotkb:Q00987) by protein kinase assay (MI:0424) (C) 2009 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.</p>

AB - <p>The E3 ubiqutin ligase, murne double-minute clone 2 (MDM2), promotes the degradation of p53 under normal homeostatic conditions. Several serine residues within the acidic domain of MDM2 are phosphorylated to maintain its activity but become hypo-phosphorylated following DNA damage, leading to inactivation of MDM2 and induction of p53. However, the signalling pathways that mediate these phosphorylation events are not fully understood. Here we show that the oncogenic and cell cycle-regulatory protein kinase, polo-like kinase-1 (PLK1), phosphorylates MDM2 at one of these residues, Ser260, and stimulates MDM2-mediated turnover of p53. These data are consistent with the idea that deregulation of PLK1 during tumourigenesis may help suppress p53 function.</p><p>Structured summary:</p><p>MINT-7266353: MDM2 (uniprotkb:Q00987) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by pull down (MI:0096)</p><p>MINT-7266344, MINT-7266329: MDM2 (uniprotkb:Q00987) physically interacts (MI:0915) with PLK1 (uniprotkb:P53350) by anti bait coimmunoprecipitation (MI:0006)</p><p>MINT-7266250: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) p53 (uniprotkb:P04637) by protein kinase assay (MI:0424)</p><p>MINT-7266241, MINT-7266318: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) MDM2 (uniprotkb:P23804) by protein kinase assay (MI:0424)</p><p>MINT-7266231, MINT-7266805, MINT-7266264, MINT-7266299: PLK1 (uniprotkb:P53350) phosphorylates (MI:0217) MDM2 (uniprotkb:Q00987) by protein kinase assay (MI:0424) (C) 2009 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.</p>

KW - p53

KW - Murne double-minute clone 2

KW - Polo-like kinase-1

KW - Phosphorylation

KW - CULTURED-CELLS

KW - PROTEIN

KW - HDM2

KW - BINDING

KW - DOMAIN

KW - PLK1

KW - SITE

KW - STABILITY

KW - PATHWAY

U2 - 10.1016/j.febslet.2009.09.057

DO - 10.1016/j.febslet.2009.09.057

M1 - Article

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 22

VL - 583

SP - 3543

EP - 3548

ER -

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