A Molecular Pathway for Myosin II Recruitment to Stress Fibers

Tojkander, Sari; Gateva, Gergana; Schevzov, Galina; Hotulainen, Pirta; Naumanen, Perttu; Martin, Claire; Gunning, Peter W.; Lappalainen, Pekka

doi:10.1016/j.cub.2011.03.007

Cited by 252 publications

(375 citation statements)

References 50 publications

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“…Indeed, forcing the mitotic and interphase formins to switch location, led to a corresponding switch in the acetylated state of Tpms within each actin-Tpm polymer, which -in turn -was shown to redirect the location of the myosin motors in the cell (Johnson et al, 2014). This aligns well with the observation that the formin Dia2 may be responsible for recruiting Tpm4.2 in an isoform-specific manner to actin filament arcs in U2OS cells, which, in turn, appears to recruit MyoIIA to these filaments (Tojkander et al, 2011). Thus, formins have been shown to play a key role in determining the Tpm composition and physical properties of an actin polymer.…”

Section: Assembly Of Specific Tpms Into Actin Filamentssupporting

confidence: 70%

“…Studies on cultured human osteosarcoma cells revealed that they express at least five Tpm isoforms that are functionally nonredundant; depletion of any one of these isoforms led to drastic defects in stress fiber assembly and/or myosin II recruitment (Tojkander et al, 2011). The Tpm isoforms also display partially distinct localization patterns within the stress fiber network, suggesting that they specify the different actin filament populations that are needed for stress fiber assembly (Fig.…”

Section: Role Of Tpm-containing Filaments In Cytoskeletal Structuresmentioning

confidence: 99%

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Tropomyosin – master regulator of actin filament function in the cytoskeleton

Gunning

Hardeman

Lappalainen

et al. 2015

Journal of Cell Science

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226

228

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Tropomyosin (Tpm) isoforms are the master regulators of the functions of individual actin filaments in fungi and metazoans. Tpms are coiled-coil parallel dimers that form a head-to-tail polymer along the length of actin filaments. Yeast only has two Tpm isoforms, whereas mammals have over 40. Each cytoskeletal actin filament contains a homopolymer of Tpm homodimers, resulting in a filament of uniform Tpm composition along its length. Evidence for this 'master regulator' role is based on four core sets of observation. First, spatially and functionally distinct actin filaments contain different Tpm isoforms, and recent data suggest that members of the formin family of actin filament nucleators can specify which Tpm isoform is added to the growing actin filament. Second, Tpms regulate wholeorganism physiology in terms of morphogenesis, cell proliferation, vesicle trafficking, biomechanics, glucose metabolism and organ size in an isoform-specific manner. Third, Tpms achieve these functional outputs by regulating the interaction of actin filaments with myosin motors and actin-binding proteins in an isoform-specific manner. Last, the assembly of complex structures, such as stress fibers and podosomes involves the collaboration of multiple types of actin filament specified by their Tpm composition. This allows the cell to specify actin filament function in time and space by simply specifying their Tpm isoform composition.

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Section: Assembly Of Specific Tpms Into Actin Filamentssupporting

confidence: 70%

Section: Role Of Tpm-containing Filaments In Cytoskeletal Structuresmentioning

confidence: 99%

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Gunning

Hardeman

Lappalainen

et al. 2015

Journal of Cell Science

Self Cite

226

228

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“…In the first case, FAs were isolated and did not occupy the whole pattern ridge or groove (figure 8e). Actin fibres connected to these FAs resembled uncontractile dorsal stress fibres [32], whereas longitudinal FAs were anchored to thicker and contractile ventral stress fibres. Therefore, on 5 mm patterns, the establishment of transverse adhesions is admissible, but their maturation is unfavoured with respect to FAs growing along the pattern.…”

Section: Discussionmentioning

confidence: 99%

Topographic cell instructive patterns to control cell adhesion, polarization and migration

Ventre

Natale

Rianna

et al. 2014

J. R. Soc. Interface.

110

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Topographic patterns are known to affect cellular processes such as adhesion, migration and differentiation. However, the optimal way to deliver topographic signals to provide cells with precise instructions has not been defined yet. In this work, we hypothesize that topographic patterns may be able to control the sensing and adhesion machinery of cells when their interval features are tuned on the characteristic lengths of filopodial probing and focal adhesions (FAs). Features separated by distance beyond the length of filopodia cannot be readily perceived; therefore, the formation of new adhesions is discouraged. If, however, topographic features are separated by a distance within the reach of filopodia extension, cells can establish contact between adjacent topographic islands. In the latter case, cell adhesion and polarization rely upon the growth of FAs occurring on a specific length scale that depends on the chemical properties of the surface. Topographic patterns and chemical properties may interfere with the growth of FAs, thus making adhesions unstable. To test this hypothesis, we fabricated different micropatterned surfaces displaying feature dimensions and adhesive properties able to interfere with the filopodial sensing and the adhesion maturation, selectively. Our data demonstrate that it is possible to exert a potent control on cell adhesion, elongation and migration by tuning topographic features' dimensions and surface chemistry.

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“…myosin, α-actinin and tropomyosin), which often have specialized functions (Quick and Skalli, 2010;Tojkander et al, 2011;Wang et al, 2011). There are differences in the biochemical and biophysical properties (e.g.…”

Section: Cellular Functions Of the Contractomementioning

confidence: 99%

“…Several F-actin-binding proteins, most notably tropomyosin, inhibit binding of myosin to the actin filament through steric hindrance, such that even the assembled actomyosin structure is not capable of generating contractility unless tropomyosin shifts its position along the filament (von der Ecken et al, 2014). A number of tropomyosin isoforms have a positive role in recruiting myosin to stress fibers (Tojkander et al, 2011). The F-actin-severing protein cofilin 1 has also been shown to compete with myosin for binding sites on F-actin (Wiggan et al, 2012).…”

Section: Contractome Subnetworkmentioning

confidence: 99%

The contractome – a systems view of actomyosin contractility in non-muscle cells

Zaidel-Bar

Guo

Luxenburg

2015

Journal of Cell Science

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Actomyosin contractility is a highly regulated process that affects many fundamental biological processes in each and every cell in our body. In this Cell Science at a Glance article and the accompanying poster, we mined the literature and databases to map the contractome of non-muscle cells. Actomyosin contractility is involved in at least 49 distinct cellular functions that range from providing cell architecture to signal transduction and nuclear activity. Containing over 100 scaffolding and regulatory proteins, the contractome forms a highly complex network with more than 230 direct interactions between its components, 86 of them involving phosphorylation. Mapping these interactions, we identify the key regulatory pathways involved in the assembly of actomyosin structures and in activating myosin to produce contractile forces within non-muscle cells at the exact time and place necessary for cellular function.

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A Molecular Pathway for Myosin II Recruitment to Stress Fibers

Abstract: These experiments identified a pathway, involving Dia2- and Arp2/3-promoted actin filament nucleation and several functionally distinct tropomyosins, that is required for generation of contractile actomyosin arrays in cells.

Cited by 252 publications

References 50 publications

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Tropomyosin – master regulator of actin filament function in the cytoskeleton

Topographic cell instructive patterns to control cell adhesion, polarization and migration

The contractome – a systems view of actomyosin contractility in non-muscle cells

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