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CCM3 is present in a folded inactive state in resting endothelial cells. In response to VEGF, CCM3 binds to and stabilizes VEGFR2, leading to an enhanced activation of the receptor and downstream signaling. The human CCM3 mutants lacking the C-terminal domain facilitate VEGFR2 endocytosis, leading to defects in VEGFR2 signaling and vascular development.
