JBC Focus on PI3-Kinase with Echelon

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Originally published In Press as doi:10.1074/jbc.M006420200 on September 29, 2000

J. Biol. Chem., Vol. 276, Issue 2, 1434-1438, January 12, 2001
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p13SUC1 and the WW Domain of PIN1 Bind to the Same Phosphothreonine-Proline Epitope*

Isabelle LandrieuDagger §||, Benoît OdaertDagger **, Jean-Michel WieruszeskiDagger , Hervé DrobecqDagger , Pierre Rousselot-PailleyDagger , Dirk InzéDagger Dagger , and Guy LippensDagger §§

From the Dagger  CNRS UMR 8525, Institut de Biologie de Lille/Pasteur Institute of Lille, 59019 Lille Cedex, France, the § Unité de Microbiologie, Faculté Universitaire des Sciences Agronomiques de Gembloux, 5030 Gembloux, Belgium, and Dagger Dagger  Laboratorium voor Genetica, Department of Plant Genetics, Flanders Interuniversity Institute for Biotechnology (VIB), Universiteit Gent, B-9000 Gent, Belgium

The WW domain of the human PIN1 and p13SUC1, a subunit of the cyclin-dependent kinase complex, were previously shown to be involved in the regulation of the cyclin-dependent kinase complex activity at the entry into mitosis, by an unresolved molecular mechanism. We report here experimental evidence for the direct interaction of p13SUC1 with a model CDC25 peptide, dependent on the phosphorylation state of its threonine. Chemical shift perturbation of backbone 1HN, 15N, and 13Calpha resonances during NMR titration experiments allows accurate identification of the binding site, primarily localized around the anion-binding site, occupied in the crystal structure of the homologous p9CKSHs2 by a sulfate molecule. The epitope recognized by p13SUC1 includes the proline at position +1 of the phosphothreonine, as was shown by the decrease in affinity for a mutated CDC25 phosphopeptide, containing an alanine/proline substitution. No direct interaction between the PIN1 WW domain or its catalytic proline cis/trans-isomerase domain and p13SUC1 was detected, but our study showed that in vitro the WW domain of the human PIN1 antagonizes the binding of the p13SUC1 to the CDC25 phosphopeptide, by binding to the same phosphoepitope. We thus propose that the full cyclin-dependent kinase complex stimulates the phosphorylation of CDC25 through binding of its p13SUC1 module to the phosphoepitope of the substrate and that the reported WW antagonism of p13SUC1-stimulated CDC25 phosphorylation is caused by competitive binding of both protein modules to the same phosphoepitope.

* This work was supported by Tournesol Grant 98.110.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Chargé de Recherches from the Fonds National de la Recherche Scientifique (Belgium).

|| To whom correspondence may be addressed. Tel.: 33 3 20871229; Fax: 33 3 20871233; E-mail: isabelle.landrieu@pasteur-lille.fr.

** Present address: Biophysical Chemistry Dept., University of Groningen, 9747 Groningen, The Netherlands.

§§ To whom correspondence may be addressed. Tel.: 33 3 20871229; Fax: 33 3 20871233; E-mail: guy.lippens@pasteur-lille.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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