Kindlin-1 regulates mitotic spindle formation by interacting with integrins and Plk-1

Hitesh Patel, Judith Zich, Bryan Serrels, Colin Rickman, Kevin G. Hardwick, Margaret C. Frame and Valerie G. Brunton ()
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Hitesh Patel: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh
Judith Zich: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Bryan Serrels: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh
Colin Rickman: Institute of Biological Chemistry, Biophysics and Bioengineering School of Engineering and Physical Sciences, Heriot-Watt University
Kevin G. Hardwick: Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
Margaret C. Frame: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh
Valerie G. Brunton: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract Kindlin-1 binds to integrins and regulates integrin activation at cell adhesions. Here we report a new function of Kindlin-1 in regulating spindle assembly. We show that Kindlin-1 localizes to centrosomes, its concentration peaking during G2/M, where it associates with various pericentriolar material proteins, including Polo-like kinase 1. Short interfering RNA-mediated depletion of Kindlin-1 increases formation of abnormal mitotic spindles and decreases cellular survival. This effect is dependent not only on the ability of Kindlin-1 to bind integrins but also on Polo-like kinase 1-mediated Kindlin-1 phosphorylation. We demonstrate that a subcellular pool of phosphorylated Kindlin-1 is located exclusively at centrosomes. Our work identifies a novel cellular role for Kindlin-1 in ensuring mitotic spindle assembly and cellular survival that is controlled by phosphorylation via Polo-like kinase 1.

Date: 2013
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DOI: 10.1038/ncomms3056

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