@article {530046,
	title = {Regulation of outside-in signaling by the β2 I domain of integrin αLβ2},
	journal = {Proc Natl Acad Sci USA},
	volume = {103},
	number = {35},
	year = {2006},
	pages = {13062-13067},
	abstract = {The adhesiveness of integrin alpha(L)beta(2) is modulated by divalent cations. We mutated three metal ion-binding sites in the beta(2) I domain. The metal ion-dependent adhesion site (MIDAS) and the ligand-induced metal-binding site are required for ligand binding and sufficient for synergism between Ca(2+) and Mg(2+). Adjacent to MIDAS (ADMIDAS) mutants are constitutively active but remain bent, with poor exposure of a beta(2) stalk region epitope. Fluorescence resonance energy transfer between fluorescent protein-fused alpha(L) and beta(2) cytoplasmic domains showed that ADMIDAS mutation abrogated ligand binding-induced spatial separation of cytoplasmic domains. Furthermore, ADMIDAS mutation abolished spreading on ligand-bearing substrates. Thus, beta(2) I domain metal ion-binding sites regulate alpha(L) I domain affinity, and the ADMIDAS is required for outside-in signaling.},
	keywords = {in file},
	author = {Chen, J. F. and Yang, W and Kim, M. and Carman, C. V. and Springer, T.A.}
}
