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- W4236325227 abstract "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." @default.
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- W4236325227 date "2011-03-01" @default.
- W4236325227 modified "2023-09-23" @default.
- W4236325227 title "P.3.006 Substance use and regional grey matter volume in individuals at high risk of psychosis" @default.
- W4236325227 doi "https://doi.org/10.1016/s0924-977x(11)70074-8" @default.
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