期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 103, 期 35, 页码 13062-13067出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0605666103
关键词
lymphocyte function-associated antigen-1; CD11a/CD18; adhesion
资金
- NCI NIH HHS [CA31798, R01 CA031798, R37 CA031798] Funding Source: Medline
- NHLBI NIH HHS [P01 HL048675, HL48675] Funding Source: Medline
The adhesiveness of integrin alpha(1)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 Ca2+ and Mg2+. 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.
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