| First Author | Vedula P | Year | 2017 |
| Journal | Elife | Volume | 6 |
| PubMed ID | 29244021 | Mgi Jnum | J:256857 |
| Mgi Id | MGI:6116984 | Doi | 10.7554/eLife.31661 |
| Citation | Vedula P, et al. (2017) Diverse functions of homologous actin isoforms are defined by their nucleotide, rather than their amino acid sequence. Elife 6:e31661 |
| abstractText | beta- and gamma-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 beta- and gamma-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 beta-actin gene critically impacts cell migration and mouse embryogenesis, we demonstrate here that generation of a mouse lacking beta-actin protein by editing beta-actin gene to encode gamma-actin protein, and vice versa, does not affect cell migration and/or organism survival. Our data suggest that the essential in vivo function of beta-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. |
