This study identifies pannexin 1 (PANX1) as a key mediator of 'find-me' signals and membrane permeability during apoptosis. PANX1 is a plasma membrane channel that facilitates the release of nucleotides such as ATP and UTP, which are crucial for recruiting phagocytes to apoptotic cells. Pharmacological inhibition and siRNA-mediated knockdown of PANX1 reduced nucleotide release and monocyte recruitment, while overexpression of PANX1 enhanced these processes. Patch-clamp recordings revealed that PANX1 is basally inactive but becomes active during apoptosis. Mechanistically, PANX1 is a target of effector caspases (caspases 3 and 7), and specific caspase-cleavage sites within PANX1 are essential for its function during apoptosis. Expression of a truncated PANX1 lacking the caspase cleavage sites resulted in a constitutively open channel. PANX1 also plays a role in the selective plasma membrane permeability of early apoptotic cells to specific dyes, such as YO-PRO-1 and TO-PRO-3. These findings highlight a novel mechanism of PANX1 activation by caspases and its critical role in the release of 'find-me' signals and membrane permeability during apoptosis.This study identifies pannexin 1 (PANX1) as a key mediator of 'find-me' signals and membrane permeability during apoptosis. PANX1 is a plasma membrane channel that facilitates the release of nucleotides such as ATP and UTP, which are crucial for recruiting phagocytes to apoptotic cells. Pharmacological inhibition and siRNA-mediated knockdown of PANX1 reduced nucleotide release and monocyte recruitment, while overexpression of PANX1 enhanced these processes. Patch-clamp recordings revealed that PANX1 is basally inactive but becomes active during apoptosis. Mechanistically, PANX1 is a target of effector caspases (caspases 3 and 7), and specific caspase-cleavage sites within PANX1 are essential for its function during apoptosis. Expression of a truncated PANX1 lacking the caspase cleavage sites resulted in a constitutively open channel. PANX1 also plays a role in the selective plasma membrane permeability of early apoptotic cells to specific dyes, such as YO-PRO-1 and TO-PRO-3. These findings highlight a novel mechanism of PANX1 activation by caspases and its critical role in the release of 'find-me' signals and membrane permeability during apoptosis.