[HTML][HTML] Identification of a urokinase receptor-integrin interaction site: promiscuous regulator of integrin function
DI Simon, Y Wei, L Zhang, NK Rao, H Xu… - Journal of Biological …, 2000 - ASBMB
Adhesion and signaling by integrins require their dynamic association with nonintegrin
membrane proteins. One such protein, the glycolipid-anchored urokinase receptor (uPAR),
associates with and modifies the function of the β 2-integrin Mac-1 (CD11b/CD18). In this
study, a critical non-I-domain binding site for uPAR on CD11b (M25; residues 424–440) is
identified by homology with a phage display peptide known to bind uPAR. Recombinant
soluble uPAR and cells expressing uPAR bound to immobilized M25, binding being …
membrane proteins. One such protein, the glycolipid-anchored urokinase receptor (uPAR),
associates with and modifies the function of the β 2-integrin Mac-1 (CD11b/CD18). In this
study, a critical non-I-domain binding site for uPAR on CD11b (M25; residues 424–440) is
identified by homology with a phage display peptide known to bind uPAR. Recombinant
soluble uPAR and cells expressing uPAR bound to immobilized M25, binding being …