The Cytoskeletal Protein α-Catenin Unfurls upon Binding to Vinculin

Rangarajan, Erumbi S.; Izard, Tina

doi:10.1074/jbc.m112.351023

Cited by 89 publications

(102 citation statements)

References 57 publications

(67 reference statements)

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“…1B, supplemental Fig. S4, A-D), and this bundled conformation of M I region is a stark contrast to the recently described unfurled or activated conformation of M I region bound to the D1 domain of vinculin (29,30) (Fig. 1D, supplemental Fig.…”

Section: Resultsmentioning

confidence: 64%

“…1E). Unraveling of the helical bundle would allow the VBS to interact with vinculin through the "helix bundle conversion" mechanism (29,30).…”

Section: Resultsmentioning

confidence: 99%

“…7A). As the activated pool of vinculin is expected to interact with the VBS of ␣-catenin (29,30), it is likely that vinculin localized at AJs also engages in actin binding, hence further reinforcing the connectivity between the cadherin-catenin complex and the F-actin. The strength of anchoring the AJ to the actin cytoskeleton can be dynamically regulated to match the actomyosin-generated tension by adjusting the polarized distribution of the cadherin-catenin complex (64), as well as the number of activated ␣-catenins and vinculins at AJs (Fig.…”

Section: Discussionmentioning

confidence: 99%

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An Autoinhibited Structure of α-Catenin and Its Implications for Vinculin Recruitment to Adherens Junctions

Ishiyama

Tanaka

Abe

et al. 2013

Journal of Biological Chemistry

111

169

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Background: ␣-Catenin is an actin-binding protein that recruits vinculin to adherens junctions. Results: An elongated autoinhibited structure of ␣-catenin indicates structural and functional coupling of its vinculin-and actin-binding mechanisms. Conclusion:The anchoring strength of adherens junctions is dynamically regulated by ␣-catenin to match the actomyosingenerated tension. Significance: Multistate conformations of ␣-catenin facilitate the direct and vinculin-assisted linkages between the cadherincatenin complex and the actin cytoskeleton.

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Section: Resultsmentioning

confidence: 64%

“…1E). Unraveling of the helical bundle would allow the VBS to interact with vinculin through the "helix bundle conversion" mechanism (29,30).…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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An Autoinhibited Structure of α-Catenin and Its Implications for Vinculin Recruitment to Adherens Junctions

Ishiyama

Tanaka

Abe

et al. 2013

Journal of Biological Chemistry

111

169

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“…Therefore, the cadherin/catenin/actin linkage may be highly dynamic, or its components may require a specific conformation not recapitulated in vitro to bind actin. This linkage may also involve additional actin-binding proteins such as activated vinculin or epithelial protein lost in neoplasm (EPLIN), which bind to α-catenin (16)(17)(18)(19)(20)(21). In addition to actin, the classical cadherin/γ-catenin (plakoglobin) complex can also associate with intermediate filaments in some instances (22,23).…”

mentioning

confidence: 99%

E-cadherin is under constitutive actomyosin-generated tension that is increased at cell–cell contacts upon externally applied stretch

Borghi

Sorokina

Shcherbakova

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

536

554

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The authors note that that in the constructs EcadTSMod, EcadTSModΔcyto, and EcadTSModΔmTFP, the Förster resonance energy transfer (FRET) acceptor fluorophore was monomeric enhanced yellow fluorescent protein (mEYFP)-not Venus as was originally reported. The photophysical properties of mEYFP and Venus, including absorption spectra, emission spectra, and fluorescence quantum yields are highly similar, leading to negligible changes in the Förster radius with the FRET donor monomeric Teal Fluorescent Protein (mTFP) (1). This substitution thus does not affect the FRET data reported in the original manuscript or their interpretation. The protein mEYFP is based on EYFP (Clontech) with the addition of the mutation A206K to suppress dimerization (2). www.pnas.org/cgi

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“…This interaction is relieved in a myosindependent manner, probably by stretching of the protein . Moreover, the vinculin-binding portion of a-catenin is linearized when it is co-crystallized with vinculin, showing directly that extensive unfolding events occur (Choi et al, 2012;Rangarajan and Izard, 2012). Additional interactions besides those with vinculin are likely to be influenced by force-dependent unfolding of a-catenin, and protein interactions with vinculin itself might be affected as well if tension across vinculin increases.…”

Section: Box 1 A-catenin Vinculin and Their Interaction Partners -Amentioning

confidence: 99%

Mechanosensitive systems at the cadherin–F-actin interface

Huveneers

Rooij

2013

Journal of Cell Science

197

189

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SummaryCells integrate biochemical and mechanical information to function within multicellular tissue. Within developing and remodeling tissues, mechanical forces contain instructive information that governs important cellular processes that include stem cell maintenance, differentiation and growth. Although the principles of signal transduction (protein phosphorylation, allosteric regulation of enzymatic activity and binding sites) are the same for biochemical and mechanical-induced signaling, the first step of mechanosensing, in which protein complexes under tension transduce changes in physical force into cellular signaling, is very different, and the molecular mechanisms are only beginning to be elucidated. In this Commentary, we focus on mechanotransduction at cell-cell junctions, aiming to comprehend the molecular mechanisms involved. We describe how different junction structures are associated with the actomyosin cytoskeleton and how this relates to the magnitude and direction of forces at cell-cell junctions. We discuss which cell-cell adhesion receptors have been shown to take part in mechanotransduction. Then we outline the force-induced molecular events that might occur within a key mechanosensitive system at cell-cell junctions; the cadherin-F-actin interface, at which a-catenin and vinculin form a central module. Mechanotransduction at cell-cell junctions emerges as an important signaling mechanism, and we present examples of its potential relevance for tissue development and disease.

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The Cytoskeletal Protein α-Catenin Unfurls upon Binding to Vinculin

Cited by 89 publications

References 57 publications

An Autoinhibited Structure of α-Catenin and Its Implications for Vinculin Recruitment to Adherens Junctions

An Autoinhibited Structure of α-Catenin and Its Implications for Vinculin Recruitment to Adherens Junctions

E-cadherin is under constitutive actomyosin-generated tension that is increased at cell–cell contacts upon externally applied stretch

Mechanosensitive systems at the cadherin–F-actin interface

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