TY - JOUR
T1 - Pattern formation and the mechanics of a motor-driven filamentous system confined by rigid membranes
AU - Tarama, Mitsusuke
AU - Shibata, Tatsuo
N1 - Funding Information:
This work was supported by the Japan Society for the Promotion of Science (JSPS) KAKENHI (Grants No. 19K14673 and No. 22K14017) and the RIKEN Special Doctoral Researcher (SPDR) Program. T.S. was supported by JSPS KAKENHI (No. JP19H00996) and JST CREST (No. JPMJCR1852), as well as by RIKEN Incentive Research Project and the core funding at RIKEN Center for Biosystems Dynamics Research. This study initiated from a conversation among M.T., S.T., Yu-Chiun Wang, and Michiko Takeda. M.T. is grateful to Yu-Chiun Wang for stimulating discussions throughout this study and constructive comments on the paper from a biological viewpoint. M.T. acknowledges Matthew S. Turner and Sonja Tarama for careful reading and productive comments on the paper.
Publisher Copyright:
© 2022 authors. Published by the American Physical Society.
PY - 2022/10
Y1 - 2022/10
N2 - Pattern formation and the mechanics of a mixture of actin filaments and myosin motors that is confined by a rigid membrane is investigated. By using a coarse-grained molecular dynamics model, we demonstrate that the competition between the depletion force and the active force of the motors gives rise to actin accumulation in the membrane vicinity. The resulting actomyosin structure exerts pressure on the membrane that, due to nematic alignment of the filaments, converges to a constant for large motor active force. The results are independent of filament length and membrane curvature, indicating the universality of this phenomenon. Thus, this paper proposes a mechanism by which the compounds of the cytoskeleton can self-organize into a higher-order structure.
AB - Pattern formation and the mechanics of a mixture of actin filaments and myosin motors that is confined by a rigid membrane is investigated. By using a coarse-grained molecular dynamics model, we demonstrate that the competition between the depletion force and the active force of the motors gives rise to actin accumulation in the membrane vicinity. The resulting actomyosin structure exerts pressure on the membrane that, due to nematic alignment of the filaments, converges to a constant for large motor active force. The results are independent of filament length and membrane curvature, indicating the universality of this phenomenon. Thus, this paper proposes a mechanism by which the compounds of the cytoskeleton can self-organize into a higher-order structure.
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U2 - 10.1103/PhysRevResearch.4.043071
DO - 10.1103/PhysRevResearch.4.043071
M3 - Article
AN - SCOPUS:85141626962
SN - 2643-1564
VL - 4
JO - Physical Review Research
JF - Physical Review Research
IS - 4
M1 - 043071
ER -