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  Investigating focal adhesion substructures by localization microscopy

Deschout, H., Platzman, I., Sage, D., Feletti, L., Spatz, J. P., & Radenovic, A. (2017). Investigating focal adhesion substructures by localization microscopy. Biophysical Journal, 113(11), 2508-2518. doi:10.1016/j.bpj.2017.09.032.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-2A65-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-2AB8-2
Genre: Journal Article

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 Creators:
Deschout, Hendrik, Author
Platzman, Ilia1, 2, Author              
Sage, Daniel, Author
Feletti, Lely, Author
Spatz, Joachim P.1, 2, Author              
Radenovic, Aleksandra, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 Abstract: Cells rely on focal adhesions (FAs) to carry out a variety of important tasks, including motion, environmental sensing, and adhesion to the extracellular matrix. Although attaining a fundamental characterization of FAs is a compelling goal, their extensive complexity and small size, which can be below the diffraction limit, have hindered a full understanding. In this study we have used single-molecule localization microscopy (SMLM) to investigate integrin β3 and paxillin in rat embryonic fibroblasts growing on two different extracellular matrix-representing substrates (i.e., fibronectin-coated substrates and specifically biofunctionalized nanopatterned substrates). To quantify the substructure of FAs, we developed a clustering method based on expectation maximization of a Gaussian mixture that accounts for localization uncertainty and background. Analysis of our SMLM data indicates that the structures within FAs, characterized as a Gaussian mixture, typically have areas between 0.01 and 1 μm2, contain 10-100 localizations, and can exhibit substantial eccentricity. Our approach based on SMLM opens new avenues for studying structural and functional biology of molecular assemblies that display substantial varieties in size, shape, and density.

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Language(s): eng - English
 Dates: 2017-05-252017-09-292017-12-052017-12-05
 Publication Status: Published in print
 Pages: 11
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 Table of Contents: -
 Rev. Method: Peer
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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 113 (11) Sequence Number: - Start / End Page: 2508 - 2518 Identifier: Other: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117