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The term phosphatidylserine receptor generally refers to cell-surface or nuclear receptors that recognize and bind to phosphatidylserine (PS), which becomes exposed on apoptotic cells. Recognition and binding to PS is a key step in the process of efferocytosis, allowing macrophages and other phagocytes to engulf and clear dying cells while releasing anti-inflammatory mediators (such as TGF-β1). The original molecule termed "phosphatidylserine receptor" (Ptdsr) was characterized as a transmembrane protein mediating recognition and engulfment of apoptotic cells. Its loss in animals causes severe developmental defects, but evidence is mixed as to its direct role in phagocytosis, and recent data suggest additional nuclear functions and equivocal roles in cell clearance. Several other proteins (notably Tim4, BAI1, Stabilin-2, and the TAM family of receptor tyrosine kinases: Tyro3, Axl, and MerTK) function as principal "phosphatidylserine receptors" in various tissues and cell types. This ambiguity should be considered when extracting information for drug discovery or functional annotation.
Stimulation or inhibition of efferocytosis (apoptotic cell uptake), immune modulation, and inhibition of inflammation.
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