Calcineurin activity is required for the completion of cytokinesis

Megan Chircop, Chandra S. Malladi, A.udrey T. Lian, Scott L. Page, Michael Zavortink, Christopher P. Gordon, Adam McCluskey, Phillip J. Robinson

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    Successful completion of cytokinesis requires the spatio-temporal regulation of protein phosphorylation and the coordinated activity of protein kinases and phosphatases. Many mitotic protein kinases are well characterized while mitotic phosphatases are largely unknown. Here, we show that the Ca2+- and calmodulin-dependent phosphatase, calcineurin (CaN), is required for cytokinesis in mammalian cells, functioning specifically at the abscission stage. CaN inhibitors induce multinucleation in HeLa cells and prolong the time cells spend connected via an extended intracellular bridge. Upon Ca2+ influx during cytokinesis, CaN is activated, targeting a set of proteins for dephosphorylation, including dynamin II (dynII). At the intracellular bridge, phospho-dynII and CaN are co-localized to dual flanking midbody rings (FMRs) that reside on either side of the central midbody ring. CaN activity and disassembly of the FMRs coincide with abscission. Thus, CaN activity at the midbody plays a key role in regulating the completion of cytokinesis in mammalian cells.
    Original languageEnglish
    Pages (from-to)3725-3737
    Number of pages13
    JournalCellular and Molecular Life Sciences
    Volume67
    Issue number21
    DOIs
    Publication statusPublished - 2010

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