Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048493 | FEBS Letters | 2012 | 6 Pages |
Scythe is a nuclear protein that has been implicated in the apoptotic process in Drosophila melanogaster; however, its role in apoptosis of mammalian cells is not fully elucidated. Here we show that cleavage of Scythe by caspase-3 occurs after activation of both the extrinsic (i.e. Fas/APO-1-mediated) and the intrinsic (i.e. staurosporine-induced) apoptosis pathway. Moreover, this caspase-dependent cleavage correlates with Scythe translocation from the nucleus to the cytosol. We also show that cytosolic re-localization of Scythe is required for Fas/APO-1-triggered phosphatidylserine (PS) exposure, a signal for macrophage clearance of apoptotic cells. Our data suggest that Scythe cleavage may represent a marker for caspase-3 activation and implicate cytosolic re-localization of Scythe in the pathway of PS exposure.
► Cleavage of Scythe/BAT3 by caspase-3 correlates with its translocation to the cytosol. ► Cytosolic Scythe is required for phosphatidylserine exposure in Fas-triggered cells. ► Cleavage of Scythe in the nucleus is a putative marker for caspase-dependent apoptosis.