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Nebulin and N-WASP Cooperate to Cause IGF-1-Induced Sarcomeric Actin Filament Formation
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Nebulin and N-WASP Cooperate to Cause IGF-1-Induced Sarcomeric Actin Filament Formation
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Journal Article
Nebulin and N-WASP Cooperate to Cause IGF-1-Induced Sarcomeric Actin Filament Formation
2010
Overview
Insulin-like growth factor 1 (IGF-1) induces skeletal muscle maturation and enlargement (hypertrophy). These responses require protein synthesis and myofibril formation (myofibrillogenesis). However, the signaling mechanisms of myofibrillogenesis remain obscure. We found that IGF-1-induced phosphatidylinositol 3-kinase-Akt signaling formed a complex of nebulin and N-WASP at the Z bands of myofibrils by interfering with glycogen synthase kinase-3β in mice. Although N-WASP is known to be an activator of the Arp2/3 complex to form branched actin filaments, the nebulin-N-WASP complex caused actin nucleation for unbranched actin filament formation from the Z bands without the Arp2/3 complex. Furthermore, N-WASP was required for IGF-1-induced muscle hypertrophy. These findings present the mechanisms of IGF-1-induced actin filament formation in myofibrillogenesis required for muscle maturation and hypertrophy and a mechanism of actin nucleation.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Actin Cytoskeleton - metabolism
/ Actins
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Bands
/ Biological and medical sciences
/ Fundamental and applied biological sciences. Psychology
/ Genomes
/ insulin-like growth factor I
/ Insulin-Like Growth Factor I - metabolism
/ Mice
/ Muscle Proteins - metabolism
/ Muscle, Skeletal - metabolism
/ Muscle, Skeletal - pathology
/ Muscles
/ Phosphatidylinositol 3-Kinase - metabolism
/ Plants
/ Protein Interaction Domains and Motifs
/ Proteins
/ Proto-Oncogene Proteins c-akt - metabolism
/ Vertebrates: osteoarticular system, musculoskeletal system
