Title

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

Authors

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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