期刊
NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-01848-y
关键词
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资金
- Marine Biological Laboratory
- University of Chicago
- NIH [5R13GM085967, CA31798, GM100160, GM092802, GM114274]
- National Center for Biological Sciences-Tata Institute of Fundamental Research
- J.C. Bose Fellowship
- HFSP [RGP0027/2012]
- NHLBI Division of Intramural Research
- Swedish Research Council [VR 524-2011-891]
- Swedish Society for Medical Research SSMF Fellowship
- Crafoord Foundation
Integrin alpha beta heterodimer cell surface receptors mediate adhesive interactions that provide traction for cell migration. Here, we test whether the integrin, when engaged to an extra-cellular ligand and the cytoskeleton, adopts a specific orientation dictated by the direction of actin flow on the surface of migrating cells. We insert GFP into the rigid, ligand-binding head of the integrin, model with Rosetta the orientation of GFP and its transition dipole relative to the integrin head, and measure orientation with fluorescence polarization microscopy. Cytoskeleton and ligand-bound integrins orient in the same direction as retrograde actin flow with their cytoskeleton-binding beta-subunits tilted by applied force. The measurements demonstrate that intracellular forces can orient cell surface integrins and support a molecular model of integrin activation by cytoskeletal force. Our results place atomic, angstrom-scale structures of cell surface receptors in the context of functional and cellular, mu m-scale measurements.
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