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Essential nucleotide- and protein-dependent functions of Actb/?-actin.


ABSTRACT: The highly similar cytoplasmic ?- and ?-actins differ by only four functionally similar amino acids, yet previous in vitro and in vivo data suggest that they support unique functions due to striking phenotypic differences between Actb and Actg1 null mouse and cell models. To determine whether the four amino acid variances were responsible for the functional differences between cytoplasmic actins, we gene edited the endogenous mouse Actb locus to translate ?-actin protein. The resulting mice and primary embryonic fibroblasts completely lacked ?-actin protein, but were viable and did not present with the most overt and severe cell and organismal phenotypes observed with gene knockout. Nonetheless, the edited mice exhibited progressive high-frequency hearing loss and degeneration of actin-based stereocilia as previously reported for hair cell-specific Actb knockout mice. Thus, ?-actin protein is not required for general cellular functions, but is necessary to maintain auditory stereocilia.

SUBMITTER: Patrinostro X 

PROVIDER: S-EPMC6077724 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Essential nucleotide- and protein-dependent functions of <i>Actb</i>/β-actin.

Patrinostro Xiaobai X   Roy Pallabi P   Lindsay Angus A   Chamberlain Christopher M CM   Sundby Lauren J LJ   Starker Colby G CG   Voytas Daniel F DF   Ervasti James M JM   Perrin Benjamin J BJ  

Proceedings of the National Academy of Sciences of the United States of America 20180716 31


The highly similar cytoplasmic β- and γ-actins differ by only four functionally similar amino acids, yet previous in vitro and in vivo data suggest that they support unique functions due to striking phenotypic differences between <i>Actb</i> and <i>Actg1</i> null mouse and cell models. To determine whether the four amino acid variances were responsible for the functional differences between cytoplasmic actins, we gene edited the endogenous mouse <i>Actb</i> locus to translate γ-actin protein. Th  ...[more]

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