The actin polymerization factor diaphanous and the actin severing protein flightless I collaborate to regulate sarcomere size.

The actin polymerization factor diaphanous and the actin severing protein flightless I collaborate to regulate sarcomere size.
Dev Biol. 2020 Sep 24;:
Authors: Deng S, Silimon RL, Balakrishnan M, Bothe I, Juros D, Soffar DB, Baylies MK
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, through controlling actin dynamics and turnover, that these actin regulators generate uniformly sized sarcomeres tuned for the muscle contractions required for flight.
PMID: 32980309 [PubMed - as supplied by publisher]

Source: Developmental Biology - September 23, 2020 Category: Biology Authors: Deng S, Silimon RL, Balakrishnan M, Bothe I, Juros D, Soffar DB, Baylies MK Tags: Dev Biol Source Type: research