eprintid: 1447206
rev_number: 60
eprint_status: archive
userid: 608
dir: disk0/01/44/72/06
datestamp: 2014-09-08 14:33:02
lastmod: 2024-07-03 11:01:17
status_changed: 2014-09-08 14:33:02
type: article
metadata_visibility: show
item_issues_count: 0
creators_name: Lewalle, A
creators_name: Fritzsche, M
creators_name: Wilson, K
creators_name: Thorogate, R
creators_name: Duke, T
creators_name: Charras, G
title: A phenomenological density-scaling approach to lamellipodial actin dynamics
ispublished: pub
divisions: UCL
divisions: B04
divisions: C06
divisions: F64
keywords: lamellipodium, actin network, photoactivation, actin dynamics
note: © 2014 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
abstract: The integration of protein function studied in vitro in a dynamic system like the cell lamellipodium remains a significant challenge. One reason is the apparent contradictory effects that perturbations of some proteins can have on the overall lamellipodium dynamics, depending on exact conditions. Theoretical modeling offers one approach for understanding the balance between the mechanisms that drive and regulate actin network growth and decay. Most models use a \bottom-up" approach, involving explicitly assembling biochemical components to simulate observable behaviour. Their correctness therefore relies on both the accurate characterisation of all the components and the completeness of the relevant processes involved. To avoid potential pitfalls due to this uncertainty, we used an alternative \top-down" approach, in which measurable features of lamellipodium behaviour, here observed in two different cell types (HL60 and B16-F1), directly inform the development of a simple phenomenological model of lamellipodium dynamics. We show that the kinetics of F-actin association and dissociation scales with the local F-actin density, with no explicit location dependence. This justifies the use of a simplified kinetic model of lamellipodium dynamics that yields predictions testable by pharmacological or genetic intervention. A length-scale parameter (the lamellipodium width), emerges from this analysis as an experimentally accessible probe of network regulatory processes.
date: 2014-10-24
publisher: The Royal Society
official_url: http://dx.doi.org/10.1098/rsfs.2014.0006
vfaculties: VMPS
vfaculties: VMPS
oa_status: green
full_text_type: pub
language: eng
primo: open
primo_central: open_green
article_type_text: Article
verified: verified_manual
elements_source: Manually entered
elements_id: 973142
doi: 10.1098/rsfs.2014.0006
lyricists_name: Charras, Guillaume
lyricists_name: Duke, Thomas
lyricists_name: Fritzsche, Marco
lyricists_name: Lewalle, Alexandre
lyricists_name: Thorogate, Richard
lyricists_name: Wilson, Kerry
lyricists_id: GCHAR39
lyricists_id: TAJDU21
lyricists_id: MFRIT58
lyricists_id: ALEWA97
lyricists_id: RTHOR67
lyricists_id: KWILS32
full_text_status: public
publication: Interface Focus
volume: 4
number: 6
article_number: 20140006
issn: 2042-8898
citation:        Lewalle, A;    Fritzsche, M;    Wilson, K;    Thorogate, R;    Duke, T;    Charras, G;      (2014)    A phenomenological density-scaling approach to lamellipodial actin dynamics.                   Interface Focus , 4  (6)    , Article 20140006.  10.1098/rsfs.2014.0006 <https://doi.org/10.1098/rsfs.2014.0006>.       Green open access   
 
document_url: https://discovery.ucl.ac.uk/id/eprint/1447206/2/LewalleEtAl_supplements.pdf
document_url: https://discovery.ucl.ac.uk/id/eprint/1447206/3/20140006.full.pdf