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Growing actin networks form lamellipodium and lamellum by self-assembly

  • Many different cell types are able to migrate by formation of a thin actin-based cytoskeletal extension. Recently, it became evident that this extension consists of two distinct substructures, designated lamellipodium and lamellum, which differ significantly in their kinetic and kinematic properties as well as their biochemical composition. We developed a stochastic two-dimensional computer simulation that includes chemical reaction kinetics, G-actin diffusion, and filament transport to investigate the formation of growing actin networks in migrating cells. Model parameters were chosen based on experimental data or theoretical considerations. In this work, we demonstrate the system's ability to form two distinct networks by self-organization. We found a characteristic transition in mean filament length as well as a distinct maximum in depolymerization flux, both within the first 1-2 microm. The separation into two distinct substructures was found to be extremely robust with respect toMany different cell types are able to migrate by formation of a thin actin-based cytoskeletal extension. Recently, it became evident that this extension consists of two distinct substructures, designated lamellipodium and lamellum, which differ significantly in their kinetic and kinematic properties as well as their biochemical composition. We developed a stochastic two-dimensional computer simulation that includes chemical reaction kinetics, G-actin diffusion, and filament transport to investigate the formation of growing actin networks in migrating cells. Model parameters were chosen based on experimental data or theoretical considerations. In this work, we demonstrate the system's ability to form two distinct networks by self-organization. We found a characteristic transition in mean filament length as well as a distinct maximum in depolymerization flux, both within the first 1-2 microm. The separation into two distinct substructures was found to be extremely robust with respect to initial conditions and variation of model parameters. We quantitatively investigated the complex interplay between ADF/cofilin and tropomyosin and propose a plausible mechanism that leads to spatial separation of, respectively, ADF/cofilin- or tropomyosin-dominated compartments. Tropomyosin was found to play an important role in stabilizing the lamellar actin network. Furthermore, the influence of filament severing and annealing on the network properties is explored, and simulation data are compared to existing experimental data.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Florian HuberORCiD, Josef Käs, Björn Stuhrmann
Open Access (DINI-Set):open_access
Open Access :Bronze - frei zugänglich aber ohne Lizenzhinweis, d.h. keine Weitergabe
Fachbereich/Einrichtung:Hochschule Düsseldorf / Fachbereich - Medien
Dokumentart:Wissenschaftlicher Artikel
Erscheinungsjahr:2008
Sprache der Veröffentlichung:Englisch
Verlag:Biophysical Society
Titel des übergeordneten Werkes (Englisch):Biophysical Journal
Band/Jahrgang/Volume:95
Heft/Ausgabe/Issue:12
Erste Seite:5508
Letzte Seite:5523
Related URL:http://www.ncbi.nlm.nih.gov/pubmed/18708450
DOI:https://doi.org/10.1529/biophysj.108.134817
ISSN:1542-0086
Freies Schlagwort / Tag:Open Archive
DDC-Klassifikation:0 Informatik, Informationswissenschaft, allgemeine Werke / 00 Informatik, Wissen, Systeme / 004 Datenverarbeitung; Informatik
Lizenz (Deutsch):keine Lizenz - nur Metadaten
Datum der Freischaltung:22.11.2021
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