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Structural insights into actin isoforms
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DOI：10.7554/eLife.82015.png)
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Abstract
En 中文
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 differences in their design principles determine the interaction with myosin motors and actin-binding proteins. 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 muscle alpha-actin (3.37 angstrom), cardiac muscle alpha-actin (3.07 angstrom), beta-actin (2.99 angstrom), and gamma-actin (3.38 angstrom) in the Mg2+center dot ADP state with their native post-translational modifications. The structures revealed isoform-specific conformations of the N-terminus that shift closer to the filament surface upon myosin binding, thereby establishing isoform-specific interfaces. Collectively, the structures of single-isotype, post-translationally modified bare skeletal muscle a-actin, cardiac muscle alpha-actin, beta-actin, and gamma-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.
Keywords:
actin
cytoskeleton
myosin
isoforms
macromolecular structure
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16