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Posteclosional phosphorylation of
myosin light chains in Drosophila.
Hiromi Y, Hotta Y
Department of Physics, University of Tokyo, Japan.
Phosphorylation of myosin light chains often plays
important roles in regulating myosin ATPase activity
during muscle contraction. Drosophila has two regulatory
myosin light chains; Lt1 which is expressed in tubular
muscles (leg muscles and direct flight muscles), and Lf1
which is specific to the fibrillar indirect flight
muscles. We found that regulatory myosin light chains are
heavily phosphorylated in mature adults, but this
phosphorylation occurs only after eclosion.
Phosphorylation accompanies the increase in the flight
ability; young adults have poor flight ability for about
one day after eclosion and have fragile myofibrils, even
though the morphogenesis of the flight muscles are
already complete at the end of the pupal stage. Animals
that harbor a small deletion in the region 11A of the
X-chromosome are viable, but their Lt1 and Lf1 myosin
light chains are hypo-phosphorylated. Mature adults of
this deletion strain are unable to fly or jump, and have
fragile myofibrils. This region is likely to include a
key gene that is responsible for the phosphorylation of
myosin light chains and the development of the flight
behavior.
PMID: USO800
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