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Ena orchestrates remodelling within the actin cytoskeleton to drive robust macrophage chemotaxis. | LitMetric

Ena orchestrates remodelling within the actin cytoskeleton to drive robust macrophage chemotaxis.

J Cell Sci

School of Cellular and Molecular Medicine, Faculty of Biomedical Sciences, University of Bristol, Bristol BS8 1TD, UK

Published: February 2019

AI Article Synopsis

  • The actin cytoskeleton is crucial for the movement of immune cells, specifically macrophages, towards areas of tissue damage or infection.
  • Research shows that the protein Ena plays a key role in forming structured filaments in the cytoskeleton, which aids macrophages in migration.
  • Ena can enhance the organization of these structures even without another protein, Fascin, leading to improved cell movement during inflammatory responses.

Article Abstract

The actin cytoskeleton is the engine that powers the inflammatory chemotaxis of immune cells to sites of tissue damage or infection. Here, we combine genetics with live imaging to investigate how cytoskeletal rearrangements drive macrophage recruitment to wounds in We find that the actin-regulatory protein Ena is a master regulator of lamellipodial dynamics in migrating macrophages, where it remodels the cytoskeleton to form linear filaments that can then be bundled together by the cross-linker Fascin (also known as Singed in flies). In contrast, the formin Dia generates rare, probing filopods for specialised functions that are not required for migration. The role of Ena in lamellipodial bundling is so fundamental that its overexpression increases bundling even in the absence of Fascin by marshalling the remaining cross-linking proteins to compensate. This reorganisation of the lamellipod generates cytoskeletal struts that push against the membrane to drive leading edge advancement and boost cell speed. Thus, Ena-mediated remodelling extracts the most from the cytoskeleton to power robust macrophage chemotaxis during their inflammatory recruitment to wounds.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6432709PMC
http://dx.doi.org/10.1242/jcs.224618DOI Listing

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