Actin-based growth cone motility and guidance

Omotade, Omotola F.; Pollitt, Stephanie L; Zheng, James

doi:10.1016/j.mcn.2017.03.001

Cited by 94 publications

(96 citation statements)

References 80 publications

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“…A neuronal growth cone at the tip of a growing axon or dendrite plays an important role in axonal guidance to a target cell (Omotade, Pollitt, & Zheng, ; Song & Poo, ; Tessier‐Lavigne & Goodman, ). The growth cones move, sense surrounding guidance cues such as attractive and repulsive factors, and find a suitable path for axonal elongation (Vitriol & Zheng, ).…”

Section: Introductionmentioning

confidence: 99%

Fascin in lamellipodia contributes to cell elasticity by controlling the orientation of filamentous actin

et al. 2019

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Fascin, an actin‐bundling protein, is present in the filopodia and lamellipodia of growth cones. However, few studies have examined lamellipodial fascin because it is difficult to observe. In this study, we evaluated lamellipodial fascin. We visualized the actin meshwork of lamellipodia in live growth cones by super‐resolution microscopy. Fascin was colocalized with the actin meshwork in lamellipodia. Ser39 of fascin is a well‐known phosphorylation site that controls the binding of fascin to actin filaments. Fluorescence recovery after photobleaching experiments with confocal microscopy showed that binding of fascin was controlled by phosphorylation of Ser39 in lamellipodia. Moreover, TPA, an agonist of protein kinase C, induced phosphorylation of fascin and dissociation from actin filaments in lamellipodia. Time series images showed that dissociation of fascin from the actin meshwork was induced by TPA. As fascin dissociated from actin filaments, the orientation of the actin filaments became parallel to the leading edge. The angle of actin filaments against the leading edge was changed from 73° to 15°. This decreased the elasticity of the lamellipodia by 40%, as measured by atomic force microscopy. These data suggest that actin bundles made by fascin contribute to elasticity of the growth cone.

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Section: Introductionmentioning

confidence: 99%

Fascin in lamellipodia contributes to cell elasticity by controlling the orientation of filamentous actin

et al. 2019

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“…The protrusion of cell surface projections such as lamellipodia and filopodia is crucial for various processes ranging from migration of individual, mesenchymal or tumour cells to neuronal growth cone advance or epithelial zippering as prerequisite, e.g., of adherens junction formation (Bachir et al, 2017;Omotade et al, 2017;Rottner et al, 2017). Lamellipodin (Lpd), a member of the Mig10/RIAM/Lpd family of adaptor proteins (MRL), localizes at the edges or tips of protruding lamellipodia and filopodia and interacts with multiple actin assembly factors involved in the regulation of dynamic actin remodelling events (Colo et al, 2012;Krause and Gautreau, 2014).…”

Section: Introductionmentioning

confidence: 99%

Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

Dimchev

Amiri

Humphries

et al. 2019

Preprint

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statement: We describe how genetic ablation of the prominent actin-and VASPbinding protein lamellipodin combined with software-aided protrusion analysis uncovers mechanistic insights into its cellular function during cell migration. 2 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.

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“…(For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.) Omotade et al, 2017). Actin shapes the tip of the growth cone, with a peripheral lamellipodium from which dynamic filopodia emerge (Bray and Chapman, 1985;Korobova and Svitkina, 2008) (Fig.…”

Section: Actin In the Growth Conementioning

confidence: 99%

The functional architecture of axonal actin

Papandréou

Leterrier

2018

Molecular and Cellular Neuroscience

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The cytoskeleton builds and supports the complex architecture of neurons. It orchestrates the specification, growth, and compartmentation of the axon: axon initial segment, axonal shaft, presynapses. The cytoskeleton must then maintain this intricate architecture for the whole life of its host, but also drive its adaptation to new network demands and changing physiological conditions. Microtubules are readily visible inside axon shafts by electron microscopy, whereas axonal actin study has long been focused on dynamic structures of the axon such as growth cones. Super-resolution microscopy and live-cell imaging have recently revealed new actin-based structures in mature axons: rings, hotspots and trails. This has caused renewed interest for axonal actin, with efforts underway to understand the precise organization and cellular functions of these assemblies. Actin is also present in presynapses, where its arrangement is still poorly defined, and its functions vigorously debated. Here we review the organization of axonal actin, focusing on recent advances and current questions in this rejuvenated field.

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Actin-based growth cone motility and guidance

Cited by 94 publications

References 80 publications

Fascin in lamellipodia contributes to cell elasticity by controlling the orientation of filamentous actin

Fascin in lamellipodia contributes to cell elasticity by controlling the orientation of filamentous actin

Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation

The functional architecture of axonal actin

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