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. 2020 Sep 19;2020:9435030. doi: 10.1155/2020/9435030

Figure 1.

Figure 1

The CD47-SIRPα interaction plays a key role in phagocytosis inhibition. The CD47-SIRPα interaction leads to the phosphorylation of two tyrosine residues in the ITIM motif included in SIRPα's cytosolic domain. Phosphorylation recruits and activates SHP1 & SHP2, signaling a cascade of events that leads to the dephosphorylation of myosin IIA and, therefore, inhibition of the cytoskeleton rearrangement, which is a necessary step for macrophages to engulf target cells. In tumor cells, the enhanced activity of the CD47-SIRPα axis is achieved by increasing CD47 expression.