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- W2950584057 abstract "Abstract β- and γ-cytoplasmic-actin are nearly indistinguishable in their amino acid sequence, but are encoded by different genes that play non-redundant biological roles. The key determinants that drive their functional distinction are unknown. Here we tested the hypothesis that β- and γ-actin functions are defined by their nucleotide, rather than their amino acid sequence, using targeted editing of the mouse genome. Although previous studies have shown that disruption of β-actin gene critically impacts cell migration and mouse embryogenesis, we demonstrate here that generation of a mouse lacking β-actin protein by editing β-actin gene to encode γ-actin protein, and vice versa, does not affect cell migration and/or organism survival. Our data suggest that the essential in vivo function of β-actin is provided by the gene sequence independent of the encoded protein isoform. We propose that this regulation constitutes a global “silent code” mechanism that controls the functional diversity of protein isoforms." @default.
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- W2950584057 date "2017-12-01" @default.
- W2950584057 modified "2023-09-28" @default.
- W2950584057 title "Diverse functions of closely homologous actin isoforms are defined by their nucleotide, rather than their amino acid sequence" @default.
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- W2950584057 doi "https://doi.org/10.1101/227546" @default.
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