Published August 1, 2012
| Version v1
Journal article
Contraction of cross-linked actomyosin bundles
Creators
- 1. WPI Advanced Institute for Materials Research (WPI-AIMR), Tohoku University, Sendai 980-8577 (Japan)
- 2. Laboratoire Physico-Chimie Curie, Institut Curie, Université Pierre et Marie Curie, CNRS UMR 168, 75005 Paris (France)
Description
Cross-linked actomyosin bundles retract when severed in vivo by laser ablation, or when isolated from the cell and micromanipulated in vitro in the presence of ATP. We identify the timescale for contraction as a viscoelastic time τ, where the viscosity is due to (internal) protein friction. We obtain an estimate of the order of magnitude of the contraction time τ ≈ 10–100 s, consistent with available experimental data for circumferential microfilament bundles and stress fibers. Our results are supported by an exactly solvable, hydrodynamic model of a retracting bundle as a cylinder of isotropic, active matter, from which the order of magnitude of the active stress is estimated. (paper)
Availability note (English)
Available from http://dx.doi.org/10.1088/1478-3975/9/4/046004Additional details
Identifiers
Publishing Information
- Journal Title
- Physical Biology (Online)
- Journal Volume
- 9
- Journal Issue
- 4
- Journal Page Range
- [11 p.]
- ISSN
- 1478-3975
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 47036295
- Subject category
- S42: ENGINEERING;
- Resource subtype / Literary indicator
- Numerical Data
- Descriptors DEI
- ATP; CONTRACTION; EXACT SOLUTIONS; EXPERIMENTAL DATA; FIBERS; FRICTION; HYDRODYNAMIC MODEL; MYOSIN; STRESSES; VISCOSITY
- Descriptors DEC
- DATA; GLOBULINS; INFORMATION; MATHEMATICAL MODELS; MATHEMATICAL SOLUTIONS; NUCLEOTIDES; NUMERICAL DATA; ORGANIC COMPOUNDS; PARTICLE MODELS; PROTEINS; STATISTICAL MODELS; THERMODYNAMIC MODEL