The protein encoded by this gene is an endothelial cell adhesion molecule that interacts preferentially with the leukocyte beta7 integrin LPAM-1 (alpha4 / beta7), L-selectin, and VLA-4 (alpha4 / beta1) on myeloid cells to direct leukocytes into mucosal and inflamed tissues.
The switch seems to be mediated by interactions between surface receptors such as uPAR and integrins, mitogenic signaling from the Ras-extracellular signal-regulated kinase (ERK) pathway, and stress induced signaling from the p38 pathway.
LFA1 (CD11a/CD18) short representation of Lymphocyte Function-associated Antigen 1, also called αLβ2 integrin
Human TGF-beta induced Ig-H3 (BIgH3) protein (4 FAS1 domains), where the FAS1 domains mediate cell adhesion through an interaction with alpha3/beta1 integrin; mutation in the FAS1 domains result in corneal dystrophy.
Within the cell, the intracellular domain of integrin binds to the cytoskeleton via adapter proteins such as talin, α-actinin, filamin and vinculin.
The second chain of αMβ2 is the common integrin β2 subunit known as CD18, and integrin αMβ2 thus belongs to the β2 subfamily (or leukocyte) integrins.
Integrin alphaXbeta2 (p150,95, CR4) is a complement receptor composed of CD11c and CD18.
LFA-1 is part of the family of leukocyte integrins that are recognised by their common β-chains (β2, CD18).
Macrophage-1 antigen (or integrin αMβ2) is a complement receptor ("CR3") consisting of CD11b (integrin αM) and CD18 (integrin β2).
RSU-1 has also been seen to act as a structural protein in integrin-mediated focal-adhesion complexes.