Faculty Publications
Dynamic Motions Of Molecular Motors In The Actin Cytoskeleton
Document Type
Article
Keywords
actin cytoskeleton, actin turnover, intracellular transport, molecular motor, myosin
Journal/Book/Conference Title
Cytoskeleton
Volume
76
Issue
11-12
First Page
517
Last Page
531
Abstract
During intracellular transport, cellular cargos, such as organelles, vesicles, and proteins, are transported within cells. Intracellular transport plays an important role in diverse cellular functions. Molecular motors walking on the cytoskeleton facilitate active intracellular transport, which is more efficient than diffusion-based passive transport. Active transport driven by kinesin and dynein walking on microtubules has been studied well during recent decades. However, mechanisms of active transport occurring in disorganized actin networks via myosin motors remain elusive. To provide physiologically relevant insights, we probed motions of myosin motors in actin networks under various conditions using our well-established computational model that rigorously accounts for the mechanical and dynamical behaviors of the actin cytoskeleton. We demonstrated that myosin motions can be confined due to three different reasons in the absence of F-actin turnover. We verified mechanisms of motor stalling using in vitro reconstituted actomyosin networks. We also found that with F-actin turnover, motors consistently move for a long time without significant confinement. Our study sheds light on the importance of F-actin turnover for effective active transport in the actin cytoskeleton.
Department
Department of Physics
Original Publication Date
11-1-2019
DOI of published version
10.1002/cm.21582
Repository
UNI ScholarWorks, Rod Library, University of Northern Iowa
Language
en
Recommended Citation
Jung, Wonyeong; Tabatabai, A. Pasha; Thomas, Jacob J.; Tabei, S. M.Ali; Murrell, Michael P.; and Kim, Taeyoon, "Dynamic Motions Of Molecular Motors In The Actin Cytoskeleton" (2019). Faculty Publications. 444.
https://scholarworks.uni.edu/facpub/444