Published October 1, 2016 | Version v1
Journal article

Isomorphic coalescence of aster cores formed in vitro from microtubules and kinesin motors

  • 1. WPI-Advanced Institute for Materials Research (WPI-AIMR), Tohoku University (Japan)
  • 2. Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University (Japan)
  • 3. Department of Biomedical Engineering, Texas A and M University, College Station, TX (United States)

Description

We report fluorescence microscopy studies of the formation of aster-like structures emerging from a cellular element-based active system and a novel analysis of the aster condensation. The system consists of rhodamine labeled microtubules which are dynamically coupled by functionalized kinesin motor proteins cross-linked via streptavidin-coated quantum dots (QDs). The aster-shaped objects contain core structures. The cores are aggregates of the QD-motor protein complexes, and result from the dynamic condensation of sub-clusters that are connected to each other randomly. The structural specificity of the aster core reflects a configuration of the initial connectivity between sub-clusters. Detailed image analysis allows us to extract a novel correlation between the condensation speed and the sub-cluster separation. The size of the core is scaled down during the condensation process, following a power law dependence on the distance between sub-clusters. The exponent of the power law is close to two, as expected from a geometric model. This single exponent common to all the contractile lines implies that there exists a time regime during which an isomorphic contraction of the aster core continues during the condensation process. We analyze the observed contraction by using a model system with potential applicability in a wide range of emergent phenomena in randomly coupled active networks, which are prevalent in the cellular environment. (paper)

Availability note (English)

Available from http://dx.doi.org/10.1088/1478-3975/13/5/056002

Additional details

Publishing Information

Journal Title
Physical Biology (Online)
Journal Volume
13
Journal Issue
5
Journal Page Range
[18 p.]
ISSN
1478-3975