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A human peptidyl–prolyl isomerase essential for regulation of mitosis

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Abstract

THE NIMA kinase is essential for progression through mitosis in Aspergillus nidulans1–6, and there is evidence for a similar pathway in other eukaryotic cells5–8. Here we describe the human protein Pinl, a peptidyl–prolyl cis/trans isomerase (PPIase) that interacts with NIMA. PPIases are important in protein folding, assembly and/or transport9–13, but none has so far been shown to be required for cell viability9–11. Pinl is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Essl/Ptfl, an essential protein in budding yeast14,15. PPIase activity is necessary for Essl/Pinl function in yeast. Depletion of Pinl/Essl from yeast or HeLa cells induces mitotic arrest, whereas HeLa cells overexpressing Pinl arrest in the G2 phase of the cell cycle. Pinl is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity.

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Author notes

  1. Steven D. Hanes: Wadsworth Center, Laboratory of Developmental Genetics, New York State Department of Health, 120 New Scotland Avenue, Albany, New York 12201, USA

Authors and Affiliations

  1. Molecular Biology and Virology Laboratory, The Salk Institute, 10010 North Torrey Pines Road, La Jolla, California, 92037, USA

    Kun Ping Lu, Steven D. Hanes & Tony Hunter

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  1. Kun Ping Lu
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  2. Steven D. Hanes
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  3. Tony Hunter
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Ping Lu, K., Hanes, S. & Hunter, T. A human peptidyl–prolyl isomerase essential for regulation of mitosis. Nature 380, 544–547 (1996). https://doi.org/10.1038/380544a0

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