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Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

Item Type:Preprint
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 barbed 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 found that genetic ablation of Lpd compromises protrusion efficiency without altering essential lamellipodial parameters, including their maximal rate of forward advancement and actin polymerization. Consistently, interference with Lpd function also decreases the frequency of Vaccinia actin tail formation, but not their speed. Moreover, computer-aided analysis of cell edge morphodynamics revealed that loss of Lpd correlates with reduced temporal maintenance of lamellipodial protrusions 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
Publisher:Cold Spring Harbor Laboratory Press
Article Number:777326
Date:20 September 2019
Official Publication:https://doi.org/10.1101/777326
Related to:
https://edoc.mdc-berlin.de/18752/Final version

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