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A ZO-1/α5β1-integrin complex regulates cytokinesis downstream of PKCε in NCI-H460 cells plated on fibronectin
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2013 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 8, no 8, e70696- p.Article in journal (Refereed) Published
Abstract [en]

Recently, we demonstrated that integrin adhesion to the extracellular matrix at the cleavage furrow is essential for cytokinesis of adherent cells. Here, we report that tight junction protein ZO-1 (Zonula Occludens-1) is required for successful cytokinesis in NCI-H460 cells plated on fibronectin. This function of ZO-1 involves interaction with the cytoplasmic domain of α5-integrin to facilitate recruitment of active fibronectin-binding integrins to the base of the cleavage furrow. In the absence of ZO-1, or a functional ZO-1/α5β1-integrin complex, proper actin-dependent constriction between daughter cells is impaired and cells fail cytokinesis. Super-resolution microscopy reveals that in ZO-1 depleted cells the furrow becomes delocalized from the matrix. We also show that PKCε-dependent phosphorylation at Serine168 is required for ZO-1 localization to the furrow and successful cell division. Altogether, our results identify a novel regulatory pathway involving the interplay between ZO-1, α5-integrin and PKCε in the late stages of mammalian cell division.

Place, publisher, year, edition, pages
2013. Vol. 8, no 8, e70696- p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-232534DOI: 10.1371/journal.pone.0070696PubMedID: 23967087OAI: oai:DiVA.org:uu-232534DiVA: diva2:748535
Available from: 2014-09-19 Created: 2014-09-19 Last updated: 2017-12-05Bibliographically approved

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Ivarsson, Ylva

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