The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.

There is a body of literature that describes the geometry and the physics of filopodia using either stochastic models or partial differential equations and elasticity and coarse-grained theory. Comparatively, there is a paucity of models focusing on the regulation of the network of proteins that con...

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Autores principales:	Federico Vaggi, Andrea Disanza, Francesca Milanesi, Pier Paolo Di Fiore, Elisabetta Menna, Michela Matteoli, Nir S Gov, Giorgio Scita, Andrea Ciliberto
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/b68d4bc1cbf4406c94c786b5380e4b0c
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spelling	oai:doaj.org-article:b68d4bc1cbf4406c94c786b5380e4b0c2021-11-18T05:50:25ZThe Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.1553-734X1553-735810.1371/journal.pcbi.1002088https://doaj.org/article/b68d4bc1cbf4406c94c786b5380e4b0c2011-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21814501/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358There is a body of literature that describes the geometry and the physics of filopodia using either stochastic models or partial differential equations and elasticity and coarse-grained theory. Comparatively, there is a paucity of models focusing on the regulation of the network of proteins that control the formation of different actin structures. Using a combination of in-vivo and in-vitro experiments together with a system of ordinary differential equations, we focused on a small number of well-characterized, interacting molecules involved in actin-dependent filopodia formation: the actin remodeler Eps8, whose capping and bundling activities are a function of its ligands, Abi-1 and IRSp53, respectively; VASP and Capping Protein (CP), which exert antagonistic functions in controlling filament elongation. The model emphasizes the essential role of complexes that contain the membrane deforming protein IRSp53, in the process of filopodia initiation. This model accurately accounted for all observations, including a seemingly paradoxical result whereby genetic removal of Eps8 reduced filopodia in HeLa, but increased them in hippocampal neurons, and generated quantitative predictions, which were experimentally verified. The model further permitted us to explain how filopodia are generated in different cellular contexts, depending on the dynamic interaction established by Eps8, IRSp53 and VASP with actin filaments, thus revealing an unexpected plasticity of the signaling network that governs the multifunctional activities of its components in the formation of filopodia.Federico VaggiAndrea DisanzaFrancesca MilanesiPier Paolo Di FioreElisabetta MennaMichela MatteoliNir S GovGiorgio ScitaAndrea CilibertoPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 7, Iss 7, p e1002088 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Federico Vaggi Andrea Disanza Francesca Milanesi Pier Paolo Di Fiore Elisabetta Menna Michela Matteoli Nir S Gov Giorgio Scita Andrea Ciliberto The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
description	There is a body of literature that describes the geometry and the physics of filopodia using either stochastic models or partial differential equations and elasticity and coarse-grained theory. Comparatively, there is a paucity of models focusing on the regulation of the network of proteins that control the formation of different actin structures. Using a combination of in-vivo and in-vitro experiments together with a system of ordinary differential equations, we focused on a small number of well-characterized, interacting molecules involved in actin-dependent filopodia formation: the actin remodeler Eps8, whose capping and bundling activities are a function of its ligands, Abi-1 and IRSp53, respectively; VASP and Capping Protein (CP), which exert antagonistic functions in controlling filament elongation. The model emphasizes the essential role of complexes that contain the membrane deforming protein IRSp53, in the process of filopodia initiation. This model accurately accounted for all observations, including a seemingly paradoxical result whereby genetic removal of Eps8 reduced filopodia in HeLa, but increased them in hippocampal neurons, and generated quantitative predictions, which were experimentally verified. The model further permitted us to explain how filopodia are generated in different cellular contexts, depending on the dynamic interaction established by Eps8, IRSp53 and VASP with actin filaments, thus revealing an unexpected plasticity of the signaling network that governs the multifunctional activities of its components in the formation of filopodia.
format	article
author	Federico Vaggi Andrea Disanza Francesca Milanesi Pier Paolo Di Fiore Elisabetta Menna Michela Matteoli Nir S Gov Giorgio Scita Andrea Ciliberto
author_facet	Federico Vaggi Andrea Disanza Francesca Milanesi Pier Paolo Di Fiore Elisabetta Menna Michela Matteoli Nir S Gov Giorgio Scita Andrea Ciliberto
author_sort	Federico Vaggi
title	The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
title_short	The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
title_full	The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
title_fullStr	The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
title_full_unstemmed	The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.
title_sort	eps8/irsp53/vasp network differentially controls actin capping and bundling in filopodia formation.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/b68d4bc1cbf4406c94c786b5380e4b0c
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The Eps8/IRSp53/VASP network differentially controls actin capping and bundling in filopodia formation.

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