Visualization of Individual Actin Filament Assembly View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2010-09-03

AUTHORS

Emmanuèle Helfer

ABSTRACT

Actin is a major protein involved in many motile processes essential for embryonic development, immune response, endo/exocytosis, cytokinesis. These processes are based on the rapid reorganization of the actin cytoskeleton in response to extracellular signaling. Indeed, in vivo observation of motile cells showed the coexistence of different actin structures: branched networks in the lamellipodium, parallel bundles in filopodia, fibers in focal adhesion complexes. Though these structures can be located in the same region of the cell, their dynamics can be very different. Real-time cell imaging showed that the filament turnover differs from one structure to the other. The molecular mechanisms that drive actin assembly/disassembly in these networks are not yet fully deciphered. How the cell controls in a concerted way the various actin motile machineries is a crucial question that is to be answered using a multidisciplinary approach. Actin dynamics was initially studied in bulk: biochemical assays were developed allowing to follow polymerization of actin filaments, and to discriminate the dynamics at each end of the filament. These studies led to an understanding of the treadmilling process of the actin filament: in presence of ATP, the net polymerization at the barbed-end balances the net depolymerization at the pointed-end. These assays are currently used to decipher the function of new actin regulating proteins. To complement the solution studies microscopy assays were developed to observe individual actin filaments. However, the first observations were done with phalloidin-stabilized filaments unable to sustain any dynamics. Only recently the microscopy technique was improved, by using excitation by an evanescent wave, allowing observation of a dynamic filament. Dynamic imaging and solution studies lead to the measurement of filament turnover dynamics. The combination with biomimetic assays consisting in in vitro reconstitution of actin structure assembly provides mechanistic insight into actin-based motile processes. More... »

PAGES

317-333

Book

TITLE

Actin-based Motility

ISBN

978-90-481-9300-4
978-90-481-9301-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-90-481-9301-1_13

DOI

http://dx.doi.org/10.1007/978-90-481-9301-1_13

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