Single-Protein Tracking to Study Protein Interactions During Integrin-Based Migration.
The Integrin Interactome. 2020-11-20; : 85-113
DOI: 10.1007/978-1-0716-0962-0_8
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Radhakrishnan AV(1)(2), Chen T(1)(2), Nunes Vicente JF(1)(2), Orré T(1)(2), Mehidi A(1)(2)(3), Rossier O(1)(2), Giannone G(4)(5).
Author information:
(1)Université de Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.
(2)CNRS, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.
(3)Department of Biochemistry, University of Geneva, Geneva, Switzerland.
(4)Université de Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France. .
(5)CNRS, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France. .
Cell migration is a complex biophysical process which involves the coordination of molecular assemblies including integrin-dependent adhesions, signaling networks and force-generating cytoskeletal structures incorporating both actin
polymerization and myosin activity. During the last decades, proteomic studies have generated impressive protein-protein interaction maps, although the subcellular location, duration, strength, sequence, and nature of these interactions are still concealed. In this chapter we describe how recent developments in superresolution microscopy (SRM) and single-protein tracking (SPT) start to unravel protein interactions and actions in subcellular molecular assemblies driving cell migration.