Polo-like kinase 1 (Plk1) mediated phosphorylation of Pin1 stabilizes Pin1 by inhibiting its ubiquitination in human cells

doi:10.1074/jbc.M504548200

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Papers In Press, published online ahead of print August 23, 2005
J. Biol. Chem, 10.1074/jbc.M504548200
Submitted on April 26, 2005
Accepted on August 23, 2005

Polo-like kinase 1 (Plk1) mediated phosphorylation of Pin1 stabilizes Pin1 by inhibiting its ubiquitination in human cells

Frank Eckerdt, Juping Yuan, Krishna Saxena, Bernd Martin, Sven Kappel, Christine Lindenau, Andrea Kramer, Steffen Naumann, Sebastian Daum, Gunter Fischer, Ivan Dikic, Manfred Kaufmann, and Klaus Strebhardt

Gynecology and Obstetrics, Medical School, J. W. Goethe-University, Molecular Oncology, Frankfurt/M, Hessen D-60590

Corresponding Author: Strebhardt{at}em.uni-frankfurt.de

The Polo-like kinase 1 (Plk1) is a key regulator of mitosis. It is reported that the human peptidyl-prolyl cis/trans isomerase (PPIase) Pin1 binds to Plk1 from mitotic cell extracts in vitro. Here we demonstrate that Ser-65 in Pin1 is the major site for Plk1-specific phosphorylation and the polo-box domain (PBD) of Plk1 is required for this phosphorylation. Interestingly, the phosphorylation of Pin1 by Plk1 does not affect its isomerase activity, rather is linked to its protein stability. Moreover, Pin1 is ubiquitinated in HeLa S3 cells and substitution of Glu for Ser-65 reduces the ubiquitination of Pin1. Furthermore, inhibition of Plk1 activity by expression of a dominant-negative form of Plk1 or by transfection of small interfering RNA (siRNA) targeted to Plk1 enhances the ubiquitination of Pin1 and subsequently reduces the amount of Pin1 in human cancer cells. Since previous reports suggested that Plk1 is a substrate of Pin1, our work adds a new dimension to this interaction of two important mitotic regulators.

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