Caspase-mediated activation of Caenorhabditis elegans CED-8 promotes apoptosis and phosphatidylserine externalization

Yu-Zen Chen, James Mapes, Eui-Seung Lee, Riley Robert Skeen-Gaar and Ding Xue ()
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Yu-Zen Chen: Cellular, and Developmental Biology, University of Colorado
James Mapes: Cellular, and Developmental Biology, University of Colorado
Eui-Seung Lee: Cellular, and Developmental Biology, University of Colorado
Riley Robert Skeen-Gaar: Cellular, and Developmental Biology, University of Colorado
Ding Xue: Cellular, and Developmental Biology, University of Colorado

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

Abstract: Abstract During apoptosis, phosphatidylserine (PS), normally restricted to the inner leaflet of the plasma membrane, is exposed on the surface of apoptotic cells and serves as an ‘eat-me’ signal to trigger phagocytosis. It is poorly understood how PS exposure is activated in apoptotic cells. Here we report that CED-8, a Caenorhabditis elegans protein implicated in controlling the kinetics of apoptosis and a homologue of the XK family proteins, is a substrate of the CED-3 caspase. Cleavage of CED-8 by CED-3 activates its proapoptotic function and generates a carboxyl-terminal cleavage product, acCED-8, that promotes PS externalization in apoptotic cells and can induce ectopic PS exposure in living cells. Consistent with its role in promoting PS externalization in apoptotic cells, ced-8 is important for cell corpse engulfment in C. elegans. Our finding identifies a crucial link between caspase activation and PS externalization, which triggers phagocytosis of apoptotic cells.

Date: 2013
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DOI: 10.1038/ncomms3726

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