The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size
| Autor: | Su Deng, Mary K. Baylies, Mridula Balakrishnan, Devin Juros, Ruth L. Silimon, Ingo Bothe, David B. Soffar |
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| Rok vydání: | 2021 |
| Předmět: |
Sarcomeres
Formins macromolecular substances Sarcomere Article 03 medical and health sciences 0302 clinical medicine Actin dynamics Myosin Animals Drosophila Proteins Actin severing protein Molecular Biology Gelsolin Actin 030304 developmental biology 0303 health sciences biology Muscles SUPERFAMILY Cell Biology Flight Animal Gene Knockdown Techniques biology.protein Biophysics Drosophila 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Dev Biol |
| ISSN: | 0012-1606 |
| DOI: | 10.1016/j.ydbio.2020.09.014 |
| Popis: | The sarcomere is the basic contractile unit of muscle, composed of repeated sets of actin thin filaments and myosin thick filaments. During muscle development, sarcomeres grow in size to accommodate the growth and function of muscle fibers. Failure in regulating sarcomere size results in muscle dysfunction; yet, it is unclear how the size and uniformity of sarcomeres are controlled. Here we show that the formin Diaphanous is critical for the growth and maintenance of sarcomere size: Dia sets sarcomere length and width through regulation of the number and length of the actin thin filaments in the Drosophila flight muscle. To regulate thin filament length and sarcomere size, Dia interacts with the Gelsolin superfamily member Flightless I (FliI). We suggest that these actin regulators, by controlling actin dynamics and turnover, generate uniformly sized sarcomeres tuned for the muscle contractions required for flight. |
| Databáze: | OpenAIRE |
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