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Helical structure of actin stress fibers and its possible contribution to inducing their direction-selective disassembly upon cell shortening

Biomechanics and modeling in mechanobiology, 2020-04, Vol.19 (2), p.543-555 [Peer Reviewed Journal]

Springer-Verlag GmbH Germany, part of Springer Nature 2019 ;Biomechanics and Modeling in Mechanobiology is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 1617-7959 ;EISSN: 1617-7940 ;DOI: 10.1007/s10237-019-01228-z ;PMID: 31549258

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Title:
Helical structure of actin stress fibers and its possible contribution to inducing their direction-selective disassembly upon cell shortening
Author: Okamoto, Tatsuki ; Matsui, Tsubasa S. ; Ohishi, Taiki ; Deguchi, Shinji
Subjects: Actin ; Actins - chemistry ; Actins - metabolism ; Adenosine Triphosphate - pharmacology ; Animals ; Atomic force microscopy ; Biological and Medical Physics ; Biomedical Engineering and Bioengineering ; Biophysics ; Cattle ; Cells, Cultured ; Contraction ; Delamination ; Disintegration ; Dismantling ; Engineering ; Fibers ; Microscopy ; Microscopy, Atomic Force ; Models, Biological ; Molecular clusters ; Needles ; Original Paper ; Protein Structure, Secondary ; Rats ; Selective disassembly ; Space life sciences ; Strain measurement ; Stress Fibers - chemistry ; Stress Fibers - metabolism ; Stress Fibers - ultrastructure ; Stress, Mechanical ; Theoretical and Applied Mechanics
Is Part Of: Biomechanics and modeling in mechanobiology, 2020-04, Vol.19 (2), p.543-555
Description: Mechanisms of the assembly of actin stress fibers (SFs) have been extensively studied, while those of the disassembly—particularly cell shortening-induced ones—remain unclear. Here, we show that SFs have helical structures composed of multi-subbundles, and they tend to be delaminated upon cell shortening. Specifically, we observed with atomic force microscopy delamination of helical SFs into their subbundles. We physically caught individual SFs using a pair of glass needles to observe rotational deformations during stretching as well as ATP-driven active contraction, suggesting that they deform in a manner reflecting their intrinsic helical structure. A minimal analytical model was then developed based on the Frenet–Serret formulas with force–strain measurement data to suggest that helical SFs can be delaminated into the constituent subbundles upon axial shortening. Given that SFs are large molecular clusters that bear cellular tension but must promptly disassemble upon loss of the tension, the resulting increase in their surface area due to the shortening-induced delamination may facilitate interaction with surrounding molecules to aid subsequent disintegration. Thus, our results suggest a new mechanism of the disassembly that occurs only in the specific SFs exposed to forced shortening.
Publisher: Berlin/Heidelberg: Springer Berlin Heidelberg
Language: English
Identifier: ISSN: 1617-7959
EISSN: 1617-7940
DOI: 10.1007/s10237-019-01228-z
PMID: 31549258
Source: MEDLINE
ProQuest Central

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Helical structure of actin stress fibers and its possible contribution to inducing their direction-selective disassembly upon cell shortening

Springer-Verlag GmbH Germany, part of Springer Nature 2019 ;Biomechanics and Modeling in Mechanobiology is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 1617-7959 ;EISSN: 1617-7940 ;DOI: 10.1007/s10237-019-01228-z ;PMID: 31549258

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