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Phosphorylation-dependent prolyl isomerization: a novel cell cycle regulatory mechanism

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Progress in Cell Cycle Research

Part of the book series: Progress in Cell Cycle Research ((PCCR))

Abstract

Protein phosphorylation by proline-directed protein kinases plays an essential role in triggering a programmed set of cell cycle events. We have recently isolated an essential and conserved mitotic regulator, Pint. Pint is a phosphorylation-dependent prolyl isomerase that specifically isomerizes the phosphorylated serine/threonine-proline bond. Pin1 also binds and regulates the function of a conserved set of mitosisspecific phosphoproteins. These results suggest phosphorylation-dependent prolyl isomerization to be a novel cell cycle regulatory mechanism. This new post-translational regulation may allow the general increase in protein phosphorylation to be converted into the organised and programmed set of structural modifications that occur during mitosis. In addition, since inhibition of Pint induces mitotic arrest and apoptosis, Pini may be a potential new drug target.

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Authors and Affiliations

  1. Cancer Biology Program Division of Hematology/Oncology, Department of Medicine, Harvard Medical School, Beth Israel Deaconess Medical Center, 330 Brookline Avenue, HIM 1047, Boston, MA, 02215, USA

    Kun Ping Lu

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  1. Centre National de la Recherche Scientifique, Roscoff, France

    Laurent Meijer  & Armelle Jézéquel  & 

  2. Centre National de la Recherche Scientifique, Université Paul Sabatier, Toulouse, France

    Bernard Ducommun

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Lu, K.P. (2000). Phosphorylation-dependent prolyl isomerization: a novel cell cycle regulatory mechanism. In: Meijer, L., Jézéquel, A., Ducommun, B. (eds) Progress in Cell Cycle Research. Progress in Cell Cycle Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4253-7_8

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