High-Affinity Bent β2-Integrin Molecules in Arresting Neutrophils Face Each Other through Binding to ICAMs In cis.
作者： Zhichao Fan , William Bill Kiosses , Hao Sun , Marco Orecchioni , Yanal Ghosheh
DOI: 10.1016/J.CELREP.2018.12.038
关键词:
摘要: Leukocyte adhesion requires β2-integrin activation. Resting integrins exist in a bent-closed conformation-i.e., not extended (E-) and high affinity (H-)-unable to bind ligand. Fully activated E+H+ integrin binds intercellular molecules (ICAMs) expressed on the opposing cell trans. E-H- transitions through E+H- or E-H+, which ICAMs same cis. Spatial patterning of is thought be required for effective arrest, but no high-resolution surface localization maps exist. Here, we developed Super-STORM by combining super-resolution microscopy with molecular modeling precisely localize identify patterns primary human neutrophils. At time neutrophil E-H+ face each other form oriented (non-random) nanoclusters. To address mechanism causing this pattern, blocked binding cis, significantly relieved face-to-face orientation.
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