Role of the elastic protein projectin in stretch activation and work output of Drosophila flight muscles.
We examine how the stretch activation response of the Drosophila indirect flight muscles (IFM) is affected by the projectin mutation bentDominant. IFM from flies heterozygous for this mutation (bentD/+) produce approximately 85% full length projectin and approximately 15% truncated projectin lacking the kinase domain and more C-terminal sequences. Passive stiffness and power output of mutant fibers is similar to that of wild-type (+/+) fibers, but the amplitude of the stretch activation response (delayed tension rise) was significantly reduced. Measurement of actomyosin kinetics by sinusoidal analysis revealed that the apparent rate constant of the delayed tension rise (2 pi b) increased in proportion to the decrease in amplitude, accounting for the near wild-type levels of power output and nearly normal flight ability. These results suggest that projectin plays a crucial role in stretch activation, possibly through its protein kinase activity, by modulating crossbridge recruitment and kinetics.
Vigoreaux
J O
JO
Department of Biology, University of Vermont, Burlington, USA.
Moore
J R
JR
Maughan
D W
DW
D000483:Alleles; D000818:Animals; D004331:Drosophila melanogaster / Q000235:genetics / Q000502:physiology*; D004548:Elasticity; D005426:Flight, Animal; D018485:Muscle Fibers, Skeletal / Q000502:physiology; D009124:Muscle Proteins / Q000235:genetics / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*
D009124:Muscle Proteins; C078033:projectin