Modelling of cross-linked actin networks - Influence of geometrical parameters and cross-link compliance

被引:14
作者
Fallqvist, B. [1 ]
Kulachenko, A. [1 ]
Kroon, M. [1 ]
机构
[1] Royal Inst Technol, Dept Solid Mech, S-10044 Stockholm, Sweden
关键词
Filamin; Actin; Cross-link; Network; Cytoskeleton; MECHANICAL-PROPERTIES; ALPHA-ACTININ; FILAMENTS; LENGTH; DYNAMICS; PROTEIN;
D O I
10.1016/j.jtbi.2014.01.032
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
A major structural component of the cell is the actin cytoskeleton, in which actin subunits are polymerised into actin filaments. These networks can be cross-linked by various types of ABPs (Actin Binding Proteins), such as Filamin A. In this paper, the passive response of cross-linked actin filament networks is evaluated, by use of a numerical and continuum network model. For the numerical model, the influence of filament length, statistical dispersion, cross-link compliance (including that representative of Filamin A) and boundary conditions on the mechanical response is evaluated and compared to experimental results. It is found that the introduction of statistical dispersion of filament lengths has a significant influence on the computed results, reducing the network stiffness by several orders of magnitude. Actin networks have previously been shown to have a characteristic transition from an initial bending-dominated to a stretching-dominated regime at larger strains, and the cross-link compliance is shown to shift this transition. The continuum network model, a modified eight-chain polymer model, is evaluated and shown to predict experimental results reasonably well, although a single set of parameters cannot be found to predict the characteristic dependence of filament length for different types of cross-links. Given the vast diversity of cross-linking proteins, the dependence of mechanical response on cross-link compliance signifies the importance of incorporating it properly in models to understand the roles of different types of actin networks and their respective tasks in the cell. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:57 / 69
页数:13
相关论文
共 29 条
[1]   A 3-DIMENSIONAL CONSTITUTIVE MODEL FOR THE LARGE STRETCH BEHAVIOR OF RUBBER ELASTIC-MATERIALS [J].
ARRUDA, EM ;
BOYCE, MC .
JOURNAL OF THE MECHANICS AND PHYSICS OF SOLIDS, 1993, 41 (02) :389-412
[2]  
Benaroya H., 2005, Probability models in engineering and science
[3]   The effect of α-actinin on the length distribution of F-actin [J].
Biron, D ;
Moses, E .
BIOPHYSICAL JOURNAL, 2004, 86 (05) :3284-3290
[4]  
BOAL D, 2002, MECH CELL
[5]   A chemo-mechanical constitutive model for transiently cross-linked actin networks and a theoretical assessment of their viscoelastic behaviour [J].
Fallqvist, B. ;
Kroon, M. .
BIOMECHANICS AND MODELING IN MECHANOBIOLOGY, 2013, 12 (02) :373-382
[6]   Phosphoinositide binding regulates α-actinin dynamics -: Mechanism for modulating cytoskeletal remodeling [J].
Fraley, TS ;
Pereira, CB ;
Tran, TC ;
Singleton, C ;
Greenwood, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (15) :15479-15482
[7]   Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy [J].
Furuike, S ;
Ito, T ;
Yamazaki, M .
FEBS LETTERS, 2001, 498 (01) :72-75
[8]   Mechanical Response of Cytoskeletal Networks [J].
Gardel, Margaret L. ;
Kasza, Karen E. ;
Brangwynne, Clifford P. ;
Liu, Jiayu ;
Weitz, David A. .
BIOPHYSICAL TOOLS FOR BIOLOGISTS, VOL 2: IN VIVO TECHNIQUES, 2008, 89 :487-+
[9]   Prestressed F-actin networks cross-linked by hinged filamins replicate mechanical properties of cells [J].
Gardel, ML ;
Nakamura, F ;
Hartwig, JH ;
Crocker, JC ;
Stossel, TP ;
Weitz, DA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (06) :1762-1767
[10]  
Gong J., 2013, PLoS One, V8, P1