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-Structure paper
タイトル | The Structural Basis of Actin Organization by Vinculin and Metavinculin. |
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ジャーナル・号・ページ | J Mol Biol, Vol. 428, Issue 1, Page 10-25, Year 2016 |
掲載日 | 2016年1月16日 |
著者 | Laura Y Kim / Peter M Thompson / Hyunna T Lee / Mihir Pershad / Sharon L Campbell / Gregory M Alushin / |
PubMed 要旨 | Vinculin is an essential adhesion protein that links membrane-bound integrin and cadherin receptors through their intracellular binding partners to filamentous actin, facilitating mechanotransduction. ...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-electron microscopy 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 that 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, providing a mechanistic framework for understanding metavinculin mutations associated with hereditary cardiomyopathies. |
リンク | J Mol Biol / PubMed:26493222 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 7.6 - 19.2 Å |
構造データ | EMDB-6446: Cryo-EM reconstruction of the vinculin-actin interface EMDB-6447, PDB-3jbk: EMDB-6449: EMDB-6450: EMDB-6451: |
化合物 | ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | STRUCTURAL PROTEIN / cytoskeleton / adhesion / actin / cell migration / mechanosensation / metavinculin / vinculin |