An interphase contractile ring reshapes primordial germ cells to allow bulk cytoplasmic remodeling.

Some cells discard undesired inherited components in bulk by forming large compartments that are subsequently eliminated. Caenorhabditis elegans primordial germ cells (PGCs) jettison mitochondria and cytoplasm by forming a large lobe that is cannibalized by intestinal cells. Although PGCs are nonmitotic, we find that lobe formation is driven by constriction of a contractile ring and requires the RhoGEF ECT-2, a RhoA activator also essential for cytokinesis. Whereas centralspindlin activates ECT-2 to promote cytokinetic contractile ring formation, we show that the ECT-2 regulator NOP-1, but not centralspindlin, is essential for PGC lobe formation. We propose that lobe contractile ring formation is locally inhibited by the PGC nucleus, which migrates to one side of the cell before the cytokinetic ring assembles on the opposite cortex. Our findings reveal how components of the cytokinetic contractile ring are reemployed during interphase to create compartments used for cellular remodeling, and they reveal differences in the spatial cues that dictate where the contractile ring will form.

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