Literature DB >> 30389091

Balance between Force Generation and Relaxation Leads to Pulsed Contraction of Actomyosin Networks.

Qilin Yu1, Jing Li1, Michael P Murrell2, Taeyoon Kim3.   

Abstract

Actomyosin contractility regulates various biological processes, including cell migration and cytokinesis. The cell cortex underlying the membrane of eukaryote cells exhibits dynamic contractile behaviors facilitated by actomyosin contractility. Interestingly, the cell cortex shows reversible aggregation of actin and myosin called "pulsed contraction" in diverse cellular phenomena, such as embryogenesis and tissue morphogenesis. Although contractile behaviors of actomyosin machinery have been studied extensively in several in vitro experiments and computational studies, none of them successfully reproduced the pulsed contraction observed in vivo. Recent experiments have suggested the pulsed contraction is dependent upon the spatiotemporal expression of a small GTPase protein called RhoA. This only indicates the significance of biochemical signaling pathways during the pulsed contraction. In this study, we reproduced the pulsed contraction with only the mechanical and dynamic behaviors of cytoskeletal elements. First, we observed that small pulsed clusters or clusters with fluctuating sizes may appear when there is subtle balance between force generation from motors and force relaxation induced by actin turnover. However, the size and duration of these clusters differ from those of clusters observed during the cellular phenomena. We found that clusters with physiologically relevant size and duration can appear only with both actin turnover and angle-dependent F-actin severing resulting from buckling induced by motor activities. We showed how parameters governing F-actin severing events regulate the size and duration of pulsed clusters. Our study sheds light on the underestimated significance of F-actin severing for the pulsed contraction observed in physiological processes.
Copyright © 2018 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2018        PMID: 30389091      PMCID: PMC6303541          DOI: 10.1016/j.bpj.2018.10.008

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


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