The actin polymerization factor Diaphanous and the actin severing protein Flightless I collaborate to regulate sarcomere size

Su Deng, Ruth L. Silimon, Mridula Balakrishnan, Ingo Bothe, Devin Juros, David B. Soffar, Mary K. Baylies

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)12-25
Number of pages14
JournalDevelopmental Biology
Volume469
DOIs
StatePublished - Jan 1 2021
Externally publishedYes

Keywords

  • Actin filaments
  • Actin polymerization
  • Actin severing
  • Diaphanous
  • Drosophila
  • Flight muscle
  • Flightless I
  • Formins
  • Gelsolin
  • Muscle maintenance
  • Sarcomere

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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