Work

Buckling-induced F-actin fragmentation modulates the contraction of active cytoskeletal networks

Year: 2017

Type: article

Abstract: Actomyosin contractility originating from interactions between F-actin and myosin facilitates various structural reorganizations of the actin cytoskeleton. Cross-linked actomyosin networks show a tendency to contract to single or multiple foci, which has been investigated extensively in numerous studies. Recently, it was suggested that suppression of F-actin buckling via an increase in bending rigidity significantly reduces network contraction. In this study, we demonstrate that networks may show the largest contraction at intermediate bending rigidity, not at the lowest rigidity, if filaments are severed by buckling arising from myosin activity as demonstrated in recent experiments; if filaments are very flexible, frequent severing events can severely deteriorate network connectivity, leading to the formation of multiple small foci and low network contraction. By contrast, if filaments are too stiff, the networks exhibit minimal contraction due to the inhibition of filament buckling. This study reveals that buckling-induced filament severing can modulate the contraction of active cytoskeletal networks, which has been neglected to date.

Source: Soft Matter

DOI: 10.1039/c6sm02703b

Authors: Jing Li, Thomas Biel, Pranith Lomada, Qilin Yu, Taeyoon Kim

Institution: Purdue University West Lafayette

Language: English

Topic: Cellular Mechanics and Interactions

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, Indiana Clinical and Translational Sciences Institute, National Institutes of Health, National Center for Advancing Translational Sciences

Awards: Indiana Clinical and Translational Sciences Institute, G801680829