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Title: Multiscale polar theory of microtubule and motor-protein assemblies

Abstract

Microtubules and motor proteins are building blocks of self-organized subcellular biological structures such as the mitotic spindle and the centrosomal microtubule array. These same ingredients can form new “bioactive” liquid-crystalline fluids that are intrinsically out of equilibrium and which display complex flows and defect dynamics. It is not yet well understood how microscopic activity, which involves polarity-dependent interactions between motor proteins and microtubules, yields such larger-scale dynamical structures. In our multiscale theory, Brownian dynamics simulations of polar microtubule ensembles driven by cross-linking motors allow us to study microscopic organization and stresses. Polarity sorting and cross-link relaxation emerge as two polar-specific sources of active destabilizing stress. On larger length scales, our continuum Doi-Onsager theory captures the hydrodynamic flows generated by polarity-dependent active stresses. Finally, the results connect local polar structure to flow structures and defect dynamics.

Authors:
 [1];  [2];  [2];  [2];  [1]
  1. New York Univ. (NYU), New York, NY (United States)
  2. Univ. of Colorado, Boulder, CO (United States)
Publication Date:
Research Org.:
New York Univ., New York, NY (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1343759
Alternate Identifier(s):
OSTI ID: 1180164
Grant/Contract Number:  
FG02-88ER25053
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Physical Review Letters
Additional Journal Information:
Journal Volume: 114; Journal Issue: 4; Journal ID: ISSN 0031-9007
Publisher:
American Physical Society (APS)
Country of Publication:
United States
Language:
English
Subject:
71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; 36 MATERIALS SCIENCE

Citation Formats

Gao, Tong, Blackwell, Robert, Glaser, Matthew A., Betterton, Meredith D., and Shelley, Michael J. Multiscale polar theory of microtubule and motor-protein assemblies. United States: N. p., 2015. Web. doi:10.1103/PhysRevLett.114.048101.
Gao, Tong, Blackwell, Robert, Glaser, Matthew A., Betterton, Meredith D., & Shelley, Michael J. Multiscale polar theory of microtubule and motor-protein assemblies. United States. doi:10.1103/PhysRevLett.114.048101.
Gao, Tong, Blackwell, Robert, Glaser, Matthew A., Betterton, Meredith D., and Shelley, Michael J. Tue . "Multiscale polar theory of microtubule and motor-protein assemblies". United States. doi:10.1103/PhysRevLett.114.048101. https://www.osti.gov/servlets/purl/1343759.
@article{osti_1343759,
title = {Multiscale polar theory of microtubule and motor-protein assemblies},
author = {Gao, Tong and Blackwell, Robert and Glaser, Matthew A. and Betterton, Meredith D. and Shelley, Michael J.},
abstractNote = {Microtubules and motor proteins are building blocks of self-organized subcellular biological structures such as the mitotic spindle and the centrosomal microtubule array. These same ingredients can form new “bioactive” liquid-crystalline fluids that are intrinsically out of equilibrium and which display complex flows and defect dynamics. It is not yet well understood how microscopic activity, which involves polarity-dependent interactions between motor proteins and microtubules, yields such larger-scale dynamical structures. In our multiscale theory, Brownian dynamics simulations of polar microtubule ensembles driven by cross-linking motors allow us to study microscopic organization and stresses. Polarity sorting and cross-link relaxation emerge as two polar-specific sources of active destabilizing stress. On larger length scales, our continuum Doi-Onsager theory captures the hydrodynamic flows generated by polarity-dependent active stresses. Finally, the results connect local polar structure to flow structures and defect dynamics.},
doi = {10.1103/PhysRevLett.114.048101},
journal = {Physical Review Letters},
number = 4,
volume = 114,
place = {United States},
year = {Tue Jan 27 00:00:00 EST 2015},
month = {Tue Jan 27 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
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Cited by: 37 works
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