bims-fascar Biomed News
on Phase separation and cellular architecture
Issue of 2019‒05‒26
four papers selected by
Victoria Yan
Max Planck Institute of Molecular Cell Biology and Genetics


  1. Proc Natl Acad Sci U S A. 2019 May 21. pii: 201814854. [Epub ahead of print]
    Weirich KL, Dasbiswas K, Witten TA, Vaikuntanathan S, Gardel ML.
      The cytoskeleton is a collection of protein assemblies that dynamically impose spatial structure in cells and coordinate processes such as cell division and mechanical regulation. Biopolymer filaments, cross-linking proteins, and enzymatically active motor proteins collectively self-organize into various precise cytoskeletal assemblies critical for specific biological functions. An outstanding question is how the precise spatial organization arises from the component macromolecules. We develop a system to investigate simple physical mechanisms of self-organization in biological assemblies. Using a minimal set of purified proteins, we create droplets of cross-linked biopolymer filaments. Through the addition of enzymatically active motor proteins, we construct composite assemblies, evocative of cellular structures such as spindles, where the inherent anisotropy drives motor self-organization, droplet deformation, and division into two droplets. These results suggest that simple physical principles underlie self-organization in complex biological assemblies and inform bioinspired materials design.
    Keywords:  active matter; actomyosin; liquid crystal; spindle; tactoids
    DOI:  https://doi.org/10.1073/pnas.1814854116
  2. Phys Rev E. 2019 Apr;99(4-1): 042601
    McDermott D, Yang Y, Reichhardt CJO, Reichhardt C.
      Using numerical simulations, we examine the dynamics of driven two-dimensional bidisperse disks flowing over quenched disorder. The system exhibits a series of distinct dynamical phases as a function of applied driving force and packing fraction, including a phase-separated state as well as a smectic state with liquid-like or polycrystalline features. At low driving forces, we find a clogged phase with an isotropic density distribution, while at intermediate driving forces the disks separate into bands of high and low densities with either liquid-like or polycrystalline structure in the high-density bands. In addition to the density phase separation, we find that in some cases there is a fractionation of the disk species, particularly when the disk size ratio is large. The species phase-separated regimes form a variety of patterns such as large disks separated by chains of smaller disks. Our results show that the formation of laning states can be enhanced by tuning the ratio of disk radius of the two species, due to the clumping of small disks in the interstitial regions between the large disks. This system could be experimentally realized using sterically interacting colloidal particles suspended in a viscous fluid driven over random pinning arrays or granular matter suspended in fluid moving over a random landscape.
    DOI:  https://doi.org/10.1103/PhysRevE.99.042601
  3. Soft Matter. 2019 May 24.
    Edozie B, Sahu S, Pitta M, Englert A, do Rosario CF, Ross JL.
      Microtubule self-organization is an essential physical process underlying several essential cellular functions, including cell division. In cell division, the dominant arrangement is the mitotic spindle, a football-shaped microtubule-based machine responsible for separating the chromosomes. We are interested in the underlying fundamental principles behind the self-organization of the spindle shape. Prior biological works have hypothesized that motor proteins control the proper formation of the spindle. Many of these motor proteins are also microtubule-crosslinkers, so it is unclear if the critical aspect is the motor activity or the crosslinking. In this study, we seek to address this question by examining the self-organization of microtubules using crosslinkers alone. We use a minimal system composed of tubulin, an antiparallel microtubule-crosslinking protein, and a crowding agent to explore the phase space of organizations as a function of tubulin and crosslinker concentration. We find that the concentration of the antiparallel crosslinker, MAP65, has a significant effect on the organization and resulted in spindle-like arrangements at relatively low concentration without the need for motor activity. Surprisingly, the length of the microtubules only moderately affects the equilibrium phase. We characterize both the shape and dynamics of these spindle-like organizations. We find that they are birefringent homogeneous tactoids. The microtubules have slow mobility, but the crosslinkers have fast mobility within the tactoids. These structures represent a first step in the recapitulation of self-organized spindles of microtubules that can be used as initial structures for further biophysical and active matter studies relevant to the biological process of cell division.
    DOI:  https://doi.org/10.1039/c8sm01835a
  4. Phys Rev E. 2019 Apr;99(4-1): 042122
    Fierro A, Coniglio A, Zannetti M.
      The ferromagnetic transition in the Ising model is the paradigmatic example of ergodicity breaking accompanied by symmetry breaking. It is routinely assumed that the thermodynamic limit is taken with free or periodic boundary conditions. More exotic symmetry-preserving boundary conditions, like cylindrical antiperiodic, are less frequently used for special tasks, such as the study of phase coexistence or the roughening of an interface. Here we show, instead, that when the thermodynamic limit is taken with these boundary conditions, a novel type of transition takes place below T_{c} (the usual Ising transition temperature) without breaking either ergodicity or symmetry. Then the low-temperature phase is characterized by a regime (condensation) of strong magnetization's fluctuations which replaces the usual ferromagnetic ordering. This is due to critical correlations perduring for all T below T_{c}. The argument is developed exactly in the d=1 case and numerically in the d=2 case.
    DOI:  https://doi.org/10.1103/PhysRevE.99.042122