Activation of beta 1 but not beta 3 integrin increases cell traction forces

Lin, Grace L.; Cohen, Daniel M.; Desai, Ravi A.; Breckenridge, Mark T.; Gao, Lin; Humphries, Martin J.; Chen, Christopher

doi:10.1016/j.febslet.2013.01.068

Cited by 72 publications

(66 citation statements)

References 41 publications

(56 reference statements)

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“…Different integrin subtypes have distinct functions; for example, a5b1 integrin determines cell adhesion, while avb3 integrin contributes to mechanotransduction in fibroblasts [22]. It has also been observed that the activation of b1, but not b3, integrin promotes the traction force in mouse embryonic fibroblasts [23]. The present results suggest that b1-specific signal pathways under hypergravity are worth further investigation.…”

Section: Discussionsupporting

confidence: 55%

Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

Zhou

Zhang

Zhuang

et al. 2015

Biochemical and Biophysical Research Communications

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Section: Discussionsupporting

confidence: 55%

Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

Zhou

Zhang

Zhuang

et al. 2015

Biochemical and Biophysical Research Communications

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“…It has been reported that extracellular stimuli leading to activation of a5b1, but not those causing activation of avb3, can trigger cell traction forces (Lin et al, 2013). In that study, the authors measured total force per cell, a parameter that is sensitive to effects on cell spreading area.…”

Section: Discussionmentioning

confidence: 99%

The integrin expression profile modulates orientation and dynamics of force transmission at cell–matrix adhesions

Balcıoğlu

Hoorn

Donato

et al. 2015

Journal of Cell Science

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Integrin adhesion receptors connect the extracellular matrix (ECM) to the cytoskeleton and serve as bidirectional mechanotransducers. During development, angiogenesis, wound healing and cancer progression, the relative abundance of fibronectin receptors, including integrins a5b1 and avb3, changes, thus altering the integrin composition of cell-matrix adhesions. Here, we show that enhanced avb3 expression can fully compensate for loss of a5b1 and other b1 integrins to support outside-in and inside-out force transmission. a5b1 and avb3 each mediate actin cytoskeletal remodeling in response to stiffening or cyclic stretching of the ECM. Likewise, a5b1 and avb3 support cellular traction forces of comparable magnitudes and similarly increase these forces in response to ECM stiffening. However, cells using avb3 respond to lower stiffness ranges, reorganize their actin cytoskeleton more substantially in response to stretch, and show more randomly oriented traction forces. Centripetal traction force orientation requires long stress fibers that are formed through the action of Rho kinase (ROCK) and myosin II, and that are supported by a5b1. Thus, altering the relative abundance of fibronectin-binding integrins in cell-matrix adhesions affects the spatiotemporal organization of force transmission.

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“…suggested that the increased spreading on fibronectin is due to the cooperative effect of α5β1 and αvβ3 integrins in promoting recognition and binding to fibronectin. The kinetics of spreading and formation of protrusions at the cell edges regulate cell traction forces, 30 which are dependent on β1 integrin activation, as determined by means of knockout cells, blocking approaches, and selective binding of this integrin type to specific ligands 12,13 . The reinforcing behavior of β1 integrin bonds appears to be necessary for spreading, since reduced surface expression of α5β1 integrins negatively impacts spreading and stress fiber formation, but increases cortical actin assembly 31 …”

Section: Discussionmentioning

confidence: 99%

Selective binding and lateral clustering ofα5β1 andαvβ3 integrins: Unraveling the spatial requirements for cell spreading and focal adhesion assembly

Schaufler

Czichos-Medda

Hirschfeld-Warnecken

et al. 2016

Cell Adhesion & Migration

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Coordination of the specific functions of α5β1 and αvβ3 integrins is crucial for the precise regulation of cell adhesion, spreading and migration, yet the contribution of differential integrin-specific crosstalk to these processes remains unclear. To determine the specific functions of αvβ3 and α5β1 integrins, we used nanoarrays of gold particles presenting immobilized, integrin-selective peptidomimetic ligands. Integrin binding to the peptidomimetics is highly selective, and cells can spread on both ligands. However, spreading is faster and the projected cell area is greater on α5β1 ligand; both depend on ligand spacing. Quantitative analysis of adhesion plaques shows that focal adhesion size is increased in cells adhering to αvβ3 ligand at 30 and 60 nm spacings. Analysis of αvβ3 and α5β1 integrin clusters indicates that fibrillar adhesions are more prominent in cells adhering to α5β1 ligand, while clusters are mostly localized at the cell margins in cells adhering to αvβ3 ligand. αvβ3 integrin clusters are more pronounced on αvβ3 ligand, though they can also be detected in cells adhering to α5β1 ligand. Furthermore, α5β1 integrin clusters are present in cells adhering to α5β1 ligand, and often colocalize with αvβ3 clusters. Taken together, these findings indicate that the activation of αvβ3 integrin by ligand binding is dispensable for initial adhesion and spreading, but essential to formation of stable focal adhesions.

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Activation of beta 1 but not beta 3 integrin increases cell traction forces

Cited by 72 publications

References 41 publications

Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

Hypergravity-induced enrichment of β1 integrin on the cell membranes of osteoblast-like cells via caveolae-dependent endocytosis

The integrin expression profile modulates orientation and dynamics of force transmission at cell–matrix adhesions

Selective binding and lateral clustering ofα5β1 andαvβ3 integrins: Unraveling the spatial requirements for cell spreading and focal adhesion assembly

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