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- W4289343311 abstract "Abstract Actin isoforms organize into distinct networks that are essential for the normal function of eukaryotic cells. Despite a high level of sequence and structure conservation, subtle changes in their design principles determine the interaction with myosin motors and actin-binding proteins. The functional diversity is further increased by posttranslational modifications (PTMs). Therefore, identifying how the structure of actin isoforms relates to function is important for our understanding of normal cytoskeletal physiology. Here, we report the high-resolution structures of filamentous skeletal α-actin (3.37Å), cardiac α-actin (3.07Å), ß-actin (2.99Å), and γ-actin (3.38Å) in the Mg 2+ ·ADP state with their native PTMs. The structures revealed isoform-specific conformations of the N-terminus that shifts closer to the filament surface upon myosin binding, thereby establishing isoform-specific interfaces. Retropropagated structural changes further show that myosin binding modulates actin filament structure. Further, our structures enabled us to reveal the location of disease-causing mutations and to analyze them with respect to known locations of PTMs. Collectively, the previously unknown structures of single-isotype, posttranslationally modified bare cardiac α-actin, ß-actin, and γ-actin reveal general principles, similarities, and differences between isoforms. They complement the repertoire of known actin structures and allow for a comprehensive understanding of in vitro and in vivo functions of actin isoforms." @default.
- W4289343311 created "2022-08-02" @default.
- W4289343311 creator A5001163039 @default.
- W4289343311 creator A5001701658 @default.
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- W4289343311 creator A5044511174 @default.
- W4289343311 creator A5048433107 @default.
- W4289343311 creator A5051917108 @default.
- W4289343311 date "2022-08-01" @default.
- W4289343311 modified "2023-09-26" @default.
- W4289343311 title "Structural Mechanisms of Actin Isoforms" @default.
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- W4289343311 doi "https://doi.org/10.1101/2022.08.01.502282" @default.
- W4289343311 hasPublicationYear "2022" @default.