Bulletin of the American Physical Society
2018 Joint Fall Meeting of the Texas Sections of APS, AAPT and Zone 13 of the SPS
Volume 63, Number 18
Friday–Saturday, October 19–20, 2018; University of Houston, Houston, Texas
Session P04: Biophysics and Soft Matter III
2:10 PM–3:22 PM,
Saturday, October 20, 2018
Science and Engineering Classroom (SEC)
Room: 102
Chair: Lloyd Lumata, University of Texas, Dallas
Abstract ID: BAPS.2018.TSF.P04.4
Abstract: P04.00004 : The role of actin filament brancher Arp2/3 in the dynamics and structures of actomyosin networks*
2:46 PM–2:58 PM
Presenter:
James Liman
(Department of Bioengineering, Rice University, Houston, Texas, Center for Theoretical Biological Physics, Rice University, Houston, Texas)
Authors:
James Liman
(Department of Bioengineering, Rice University, Houston, Texas, Center for Theoretical Biological Physics, Rice University, Houston, Texas)
Carlos A. Bueno
(Center for Theoretical Biological Physics, Rice University, Houston, Texas, Systems, Synthetic, and Physical Biology, Rice University, Houston, Texas)
Yossi Eliaz
(Center for Theoretical Biological Physics, Rice University, Houston, Texas, Department of Physics, University of Houston, Houston, Texas)
Peter G. Wolynes
(Center for Theoretical Biological Physics, Rice University, Houston, Texas)
Herbert Levine
(Department of Bioengineering, Rice University, Houston, Texas, Center for Theoretical Biological Physics, Rice University, Houston, Texas)
Margaret S. Cheung
(Center for Theoretical Biological Physics, Rice University, Houston, Texas, Department of Physics, University of Houston, Houston, Texas)
Actomyosin network contractility underlies the motility and division of a cell, involving contraction and expansion that are driven by active protein motors and actin treadmilling. In this work, we present novel computational and theoretical approaches to model contractility and growth in actomyosin networks and evaluate the spatiotemporal patterns of actin reorganization. We consider two different actomyosin network morphologies, unbranched and branched. For the unbranched case, the system includes motor proteins (non-muscle myosin IIA (NMIIA)) and cross-linker proteins (α-actinin). For the branched case, the system includes a third component—Arp2/3 complexes—that allows us to investigate the role of branching in actomyosin contractility. We observe that linkers modulate contraction in the unbranched and the branched actomyosin networks. The branched actomyosin networks relax more slowly than their unbranched counterparts. However, the branched networks show pronounced convulsive contractions. We expect our results to give an insight into the importance of the branched morphological formation in enhancing contractility of the actomyosin networks.
*This work is supported by the National Science Foundation CHE 1743392 and the Center for Theoretical Biological Physics PHY 1427654.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2018.TSF.P04.4
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