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Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

Item Type:Article
Title:Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation
Creators Name:Dimchev, G. and Amiri, B. and Humphries, A.C. and Schaks, M. and Dimchev, V. and Stradal, T.E.B. and Faix, J. and Krause, M. and Way, M. and Falcke, M. and Rottner, K.
Abstract:Efficient migration on adhesive surfaces involves the protrusion of lamellipodial actin networks and their subsequent stabilization by nascent adhesions. The actin binding protein lamellipodin (Lpd) is thought to play a critical role in lamellipodium protrusion, by delivering Ena/VASP proteins onto the growing plus ends of actin filaments and by interacting with the WAVE regulatory complex (WRC), an activator of the Arp2/3 complex, at the leading edge. Using B16-F1 melanoma cell lines, we demonstrate that genetic ablation of Lpd compromises protrusion efficiency and coincident cell migration without altering essential parameters of lamellipodia, including their maximal rate of forward advancement and actin polymerization. We also confirmed lamellipodia and migration phenotypes with CRISPR/Cas9-mediated Lpd knockout Rat2 fibroblasts, excluding cell type-specific effects. Moreover, computer-aided analysis of cell edge morphodynamics on B16-F1 cell lamellipodia revealed that loss of Lpd correlates with reduced temporal protrusion maintenance as a prerequisite of nascent adhesion formation. We conclude that Lpd optimizes protrusion and nascent adhesion formation by counteracting frequent, chaotic retraction and membrane ruffling.
Keywords:Lamellipodium, VASP, Arp2/3, WAVE Regulatory Complex, Animals, Mice
Source:Journal of Cell Science
ISSN:0021-9533
Publisher:Company of Biologists
Volume:133
Number:7
Page Range:jcs239020
Date:9 April 2020
Official Publication:https://doi.org/10.1242/jcs.239020
PubMed:View item in PubMed
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https://edoc.mdc-berlin.de/18449/Preprint version

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