Every day, billions of new cells are produced in our bodies, and an equivalent number must die. Normally this occurs by apoptosis (1), during which the chromatin compacts against the nuclear envelope, followed rapidly by nuclear fragmentation and budding into multiple membrane-bound apoptotic bodies. This “dance of death” results from the activation of certain proteases known as caspases, culminating in activation of effector caspases-3 and -7, which target hundreds of vital cellular proteins. Importantly, because there is no cell membrane rupture, apoptotic cell death provokes no inflammatory response, in contrast to cell death by necrosis, necroptosis, or pyroptosis. However, in our bodies, as in our communities, proper disposal of detritus is vital for our health. Thus, the apoptotic corpses are recognized and rapidly removed by phagocytic cells, a process termed efferocytosis. Much of what we currently understand about efferocytosis has been established by research conducted in Shigekazu Nagata’s laboratory, including the PNAS paper by Segawa et al. (2), which describes how efferocytosis can be turned upon live B cell progenitors, provoking severe B cell lymphopenia. Disposal of apoptotic bodies by phagocytes mandates that they are clearly distinguishable from normal cells. The critical (eat me) signal is the presence of phosphatidylserine (PtdSer) in the outer leaflet of the plasma membrane (3⇓–5). In healthy cells, nearly all PtdSer molecules (and other aminophospholids) are confined to the inner leaflet of the plasma membrane due to the activity of ATP-dependent phospholipid flippases, including the P4-type ATPases ATP11A and ATP11C. Together with their chaperone, CDC50A, these proteins specifically translocate PtdSer from the outer to the inner leaflet of the plasma membrane (Fig. 1 A ). Fig. 1. Phospholipid redistribution dynamics at the plasma membrane. ( A ) In normal cells, flippases ATP11A and ATP11C, heterodimerized with their chaperone, CDC50A, continuously translocate PtdSer from the outer to the … [↵][1]1Email: cory{at}wehi.edu.au. [1]: #xref-corresp-1-1