Morphological control enables nanometer-scale dissection of cell-cell signaling complexes

Liam P. Dow, Guido Gaietta, Yair Kaufman, Mark F. Swift, Moara Lemos, Kerry Lane, Matthew Hopcroft, Armel Bezault, Cécile Sauvanet, Niels Volkmann (), Beth L. Pruitt () and Dorit Hanein ()
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Liam P. Dow: University of California
Guido Gaietta: Scintillon Institute
Yair Kaufman: University of California
Mark F. Swift: Scintillon Institute
Moara Lemos: Institut Pasteur, CNRS UMR3528, Structural Studies of Macromolecular Machines in Cellulo Unit
Kerry Lane: University of California
Matthew Hopcroft: University of California
Armel Bezault: Institut Pasteur, CNRS UMR3528, Structural Studies of Macromolecular Machines in Cellulo Unit
Cécile Sauvanet: Institut Pasteur, CNRS UMR3528, Structural Studies of Macromolecular Machines in Cellulo Unit
Niels Volkmann: Scintillon Institute
Beth L. Pruitt: University of California
Dorit Hanein: Scintillon Institute

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Protein micropatterning enables robust control of cell positioning on electron-microscopy substrates for cryogenic electron tomography (cryo-ET). However, the combination of regulated cell boundaries and the underlying electron-microscopy substrate (EM-grids) provides a poorly understood microenvironment for cell biology. Because substrate stiffness and morphology affect cellular behavior, we devised protocols to characterize the nanometer-scale details of the protein micropatterns on EM-grids by combining cryo-ET, atomic force microscopy, and scanning electron microscopy. Measuring force displacement characteristics of holey carbon EM-grids, we found that their effective spring constant is similar to physiological values expected from skin tissues. Despite their apparent smoothness at light-microscopy resolution, spatial boundaries of the protein micropatterns are irregular at nanometer scale. Our protein micropatterning workflow provides the means to steer both positioning and morphology of cell doublets to determine nanometer details of punctate adherens junctions. Our workflow serves as the foundation for studying the fundamental structural changes governing cell-cell signaling.

Date: 2022
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DOI: 10.1038/s41467-022-35409-9

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