uPA binding to uPAR stimulates the interaction of uPAR with integral membrane proteins, such as integrins, which signal intracellularly to promote cytoskeletal reorganization and cell migration. The urokinase receptor (uPAR) consists of three internally disulfide-bonded domains and is attached to the cell surface by a glycosyl phosphatidylinositol (GPI) anchor. Upon cleavage of the GPI, uPAR is released from the plasma membrane into its soluble form. Both uPAR and soluble uPAR (suPAR) can be cleaved in the region that links domains D1 to D2 to yield a D1 and D2D3 fragment, which has direct chemotactic activity.
CD87; Monocyte activation antigen Mo3; PLAUR; U-PAR; u-plasminogen activator receptor form 2; UPAR; URKR; Urokinase plasminogen activator surface receptor; urokinase-type plasminogen activator (uPA) receptor
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