Actin stress fibers – assembly, dynamics and biological roles

Tojkander, Sari; Gateva, Gergana; Lappalainen, Pekka

doi:10.1242/jcs.098087

Cited by 900Cellular Mechanics and InteractionsSkin and Cellular Biology ResearchMicrotubule and mitosis dynamics

Actin stress fibers – assembly, dynamics and biological roles

Tojkander, Sari, Gateva, Gergana, Lappalainen, Pekka·2012·Journal of Cell Science

DOI 10.1242/jcs.098087

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Abstract

Actin filaments assemble into diverse protrusive and contractile structures to provide force for a number of vital cellular processes. Stress fibers are contractile actomyosin bundles found in many cultured non-muscle cells, where they have a central role in cell adhesion and morphogenesis. Focal-adhesion-anchored stress fibers also have an important role in mechanotransduction. In animal tissues, stress fibers are especially abundant in endothelial cells, myofibroblasts and epithelial cells. Importantly, recent live-cell imaging studies have provided new information regarding the mechanisms of stress fiber assembly and how their contractility is regulated in cells. In addition, these studies might elucidate the general mechanisms by which contractile actomyosin arrays, including muscle cell myofibrils and cytokinetic contractile ring, can be generated in cells. In this Commentary, we discuss recent findings concerning the physiological roles of stress fibers and the mechanism by which these structures are generated in cells.

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Bounds of the bending force applied to the first anchor point were determined using literature values, resulting in P1 = Pmax = 0.12-2.25 nN.
“Bounds of the bending force applied to the first anchor point were determined using literature values for the force exerted by each active myosin-II dimer, the number of myosin-II dimers Nmyo per actin filament and the number of actin filaments in each stress filament Nactin (Eq. 3 in Appendix A) [35, 36], resulting in P1 = Pmax = 0.12–2.25 nN.”
From Macrophages bend long fibres with flexural rigidity lower than 3 mN·nm2 to avoid frustrated phagocytosis (2026) · cites this paper as [35]

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Authors: Tojkander, S., Gateva, G., & Lappalainen, P.
Affiliations: University of Helsinki (FI)
Corresponding author: Lappalainen, Pekka
ORCID: Tojkander, Sari
Lappalainen, Pekka
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2012-01-01
Volume: 125
Issue: Pt 8
Pages: 1855-64
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.098087
OpenAlex: W2151492748
Cited by: 900
References: 155
Citations by year: 2026: 23 · 2025: 59 · 2024: 68 · 2023: 59 · 2022: 61 · 2021: 100 · 2020: 99 · 2019: 85 · 2018: 53 · 2017: 73 · 2016: 66 · 2015: 66 · 2014: 48 · 2013: 35 · 2012: 5
FWCI: 23.20
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Funders: Academy of Finland
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: stress fibers, actomyosin contractility, focal adhesions, mechanotransduction, cell adhesion, cell morphogenesis, endothelial cells, myofibroblasts, epithelial cells, contractile ring, myofibrils, non-muscle cells
MeSH terms: Actins, Animals, Cell Adhesion, Cell Movement, Humans, Stress Fibers, Mechanotransduction, Cellular

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Actin stress fibers – assembly, dynamics and biological roles

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