Calcineurin activity is required for the completion of cytokinesis |
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Authors: | Megan Chircop Chandra S Malladi Audrey T Lian Scott L Page Michael Zavortink Christopher P Gordon Adam McCluskey Phillip J Robinson |
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Institution: | (1) Children’s Medical Research Institute, The University of Sydney, 214 Hawkesbury Road, Westmead, NSW, 2145, Australia;(2) Chemistry, School of Environmental and Life Sciences, The University of Newcastle, Callaghan, NSW, 2308, Australia |
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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. |
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