Cytosolic actin isoforms form networks with different rheological properties that indicate specific biological function

Peter Nietmann, Kevin Kaub, Andrejus Suchenko, Susanne Stenz, Claas Warnecke, Mohan K. Balasubramanian and Andreas Janshoff ()
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Peter Nietmann: University of Goettingen
Kevin Kaub: University of Goettingen
Andrejus Suchenko: University of Warwick
Susanne Stenz: University of Goettingen
Claas Warnecke: University of Goettingen
Mohan K. Balasubramanian: University of Warwick
Andreas Janshoff: University of Goettingen

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract The implications of the existence of different actins expressed in epithelial cells for network mechanics and dynamics is investigated by microrheology and confocal imaging. γ-actin predominately found in the apical cortex forms stiffer networks compared to β-actin, which is preferentially organized in stress fibers. We attribute this to selective interactions with Mg2+-ions interconnecting the filaments’ N-termini. Bundling propensity of the isoforms is different in the presence of Mg2+-ions, while crosslinkers such as α-actinin, fascin, and heavy meromyosin alter the mechanical response independent of the isoform. In the presence of myosin, β-actin networks show a large number of small contraction foci, while γ-actin displays larger but fewer foci indicative of a stronger interaction with myosin motors. We infer that subtle changes in the amino acid sequence of actin isoforms lead to alterations of the mechanical properties on the network level with potential implications for specific biological functions.

Date: 2023
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DOI: 10.1038/s41467-023-43653-w

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