Vinculin and metavinculin: Oligomerization and interactions with F‐actin

Thompson, Peter M.; Tolbert, Caitlin E.; Campbell, Sharon L.

doi:10.1016/j.febslet.2013.02.042

Cited by 36 publications

(28 citation statements)

References 88 publications

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“…This structural change accounts for the altered tilt and twist of cofilin decorated filaments observed by EM 60,61 , Cryo-EM 59 and AFM 40 . No such tilt and twist in actin filaments decorated with MVT is observed by EM 7,12 . This is consistent with our finding that the D-loop and other structures are only mildly altered when actin is decorated with MVT.…”

Section: Discussionmentioning

confidence: 83%

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Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments

Durer

McGillivary

Kang

et al. 2015

Journal of Molecular Biology

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Vinculin is an abundant protein found at cell-cell and cell-extracellular matrix junctions. In muscles, a longer splice-isoform of vinculin, metavinculin, is also expressed. The metavinculin-specific insert is part of the C-terminal tail domain, the actin-binding site of both isoforms. Mutations in the metavinculin-specific insert are linked to heart disease such as dilated cardiomyopathies. Vinculin tail domain (VT) both binds and bundles actin filaments. Metavinculin tail domain (MVT) binds actin filaments in a similar orientation but does not bundle filaments. Recently, MVT was reported to sever actin filaments. In this work, we asked how MVT influences F-actin alone or in combination with VT. Cosedimentation and limited proteolysis experiments indicated a similar actin binding affinity and mode for both VT and MVT. In real time TIRF microscopy experiments MVT’s severing activity was negligible. Instead, we found that MVT binding caused a two-fold reduction in F-actin’s bending persistence length and increased susceptibility to breakage. Perhaps MVT allows the load of muscle contraction to act as a signal to reorganize actin filaments. Using mutagenesis and site-directed labeling with fluorescence probes, we determined that MVT alters actin interprotomer contacts and dynamics, which presumably reflect the observed changes in bending persistence length. Finally, we found that MVT decreases the density and thickness of actin filament bundles generated by VT. Altogether, our data suggest that MVT alters actin filament flexibility and tunes filament organization in the presence of VT. Both of these activities are potentially important for muscle cell function.

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Section: Discussionmentioning

confidence: 83%

“…The helices are flanked by a so-called N-terminal strap and C-terminal arm, which interact with each other and a subset of the VT helices. The VT can dimerize in a number of configurations, one of which relies on a cryptic binding site that is revealed upon binding to actin and results in bundling 7,8 .…”

Section: Introductionmentioning

confidence: 99%

Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments

Durer

McGillivary

Kang

et al. 2015

Journal of Molecular Biology

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“…The loss of Vinculin inhibits cell adhesion and diffusion. The absence of this protein results in lower cell dissemination on the material to be assessed and scarce formation of focal adhesions [27]; therefore, the images obtained in this study demonstrated that the group treated with MTA exhibited the lowest expression of Vinculin.…”

Section: Discussionmentioning

confidence: 90%

Cytotoxicity and Initial Biocompatibility of Endodontic Biomaterials (MTA and Biodentine™) Used as Root-End Filling Materials

Escobar‐García

Aguirre-López

Méndez-González

et al. 2016

BioMed Research International

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Objective. The aim of this study was to evaluate the cytotoxicity and cellular adhesion of Mineral Trioxide Aggregate (MTA) and Biodentine (BD) on periodontal ligament fibroblasts (PDL). Methods. PDL cells were obtained from nonerupted third molars and cultured; MTS cellular profusion test was carried out in two groups: MTA and BD, with respective controls at different time periods. Also, the LIVE/DEAD assay was performed at 24 h. For evaluation of cellular adhesion, immunocytochemistry was conducted to discern the expression of Integrin β1 and Vinculin at 12 h and 24 h. Statistical analysis was performed by the Kruskal-Wallis and Mann-Whitney U tests. Results. MTA and BD exhibited living cells up to 7 days. More expressions of Integrin β1 and Vinculin were demonstrated in the control group, followed by BD and MTA, which also showed cellular loss and morphological changes. There was a significant difference in the experimental groups cultured for 5 and 7 days compared with the control, but there was no significant statistical difference between both cements. Conclusions. Neither material was cytotoxic during the time evaluated. There was an increase of cell adhesion through the expression of focal contacts observed in the case of BD, followed by MTA, but not significantly.

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“…The structure of the actin-induced Vt dimer (reviewed in ref. 58 ) remains an important subject for future investigations.…”

Section: Discussionmentioning

confidence: 99%

The Structural Basis of Actin Organization by Vinculin and Metavinculin

Kim

Thompson

Lee

et al. 2016

Journal of Molecular Biology

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Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. Here we present an 8.5 Å resolution cryo-EM reconstruction and pseudo-atomic model of the vinculin tail (Vt) domain bound to F-actin. Upon actin engagement, the N-terminal “strap” and helix 1 are displaced from the Vt helical bundle to mediate actin bundling. We find that an analogous conformational change also occurs in the H1’ helix of the tail domain of metavinculin (MVt) upon actin binding, a muscle-specific splice isoform which suppresses actin bundling by Vt. These data support a model in which metavinculin tunes the actin bundling activity of vinculin in a tissue-specific manner and provide a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies.

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Vinculin and metavinculin: Oligomerization and interactions with F‐actin

Cited by 36 publications

References 88 publications

Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments

Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments

Cytotoxicity and Initial Biocompatibility of Endodontic Biomaterials (MTA and Biodentine™) Used as Root-End Filling Materials

The Structural Basis of Actin Organization by Vinculin and Metavinculin

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