Aurora A kinase modulates actin cytoskeleton through phosphorylation of Cofilin: Implication in the mitotic process

    Authors

    L. Ritchey;R. Chakrabarti

    Comments

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    Abbreviated Journal Title

    Biochim. Biophys. Acta-Mol. Cell Res.

    Keywords

    Aurora A kinase; Cofilin; Mitosis; Phosphorylation; Actin cytoskeleton; TRANS-GOLGI NETWORK; A KINASE; LIM-KINASE; CENTROSOME MATURATION; PROTEIN-KINASE; BREAST-CANCER; CELLS; MITOSIS; SPINDLE; REORGANIZATION; Biochemistry & Molecular Biology; Cell Biology

    Abstract

    Aurora A kinase regulates early mitotic events through phosphorylation and activation of a variety of proteins. Specifically, Aur-A is involved in centrosomal separation and formation of mitotic spindles in early prophase. The effect of Aur-A on mitotic spindles is mediated by the modulation of microtubule dynamics and association with microtubule binding proteins. In this study we show that Aur-A exerts its effects on spindle organization through the regulation of the actin cytoskeleton. Aurora A phosphorylates Cofilin at multiple sites including S-3 resulting in the inactivation of its actin depolymerizing function. Aur-A interacts with Cofilin in early mitotic phases and regulates its phosphorylation status. Cofilin phosphorylation follows a dynamic pattern during the progression of prophase to metaphase. Inhibition of Aur-A activity induced a delay in the progression of prophase to metaphase. Aur-A inhibitor also disturbed the pattern of Cofilin phosphorylation, which correlated with the mitotic delay. Our results establish a novel function of Aur-A in the regulation of actin cytoskeleton reorganization, through Cofilin phosphorylation during early mitotic stages. (C) 2014 Elsevier B.V. All rights reserved.

    Journal Title

    Biochimica Et Biophysica Acta-Molecular Cell Research

    Volume

    1843

    Issue/Number

    11

    Publication Date

    1-1-2014

    Document Type

    Article

    Language

    English

    First Page

    2719

    Last Page

    2729

    WOS Identifier

    WOS:000342527800033

    ISSN

    0167-4889

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