|Title:||Tks5 and Dynamin-2 enhance actin bundle rigidity in invadosomes to promote myoblast fusion||Authors:||Chuang, Mei-Chun
Ohniwa, Ryosuke L
|Issue Date:||6-May-2019||Publisher:||ROCKEFELLER UNIV PRESS||Journal Volume:||218||Journal Issue:||5||Start page/Pages:||1670||Source:||The Journal of cell biology||Abstract:||
Skeletal muscle development requires the cell-cell fusion of differentiated myoblasts to form muscle fibers. The actin cytoskeleton is known to be the main driving force for myoblast fusion; however, how actin is organized to direct intercellular fusion remains unclear. Here we show that an actin- and dynamin-2-enriched protrusive structure, the invadosome, is required for the fusion process of myogenesis. Upon differentiation, myoblasts acquire the ability to form invadosomes through isoform switching of a critical invadosome scaffold protein, Tks5. Tks5 directly interacts with and recruits dynamin-2 to the invadosome and regulates its assembly around actin filaments to strengthen the stiffness of dynamin-actin bundles and invadosomes. These findings provide a mechanistic framework for the acquisition of myogenic fusion machinery during myogenesis and reveal a novel structural function for Tks5 and dynamin-2 in organizing actin filaments in the invadosome to drive membrane fusion.
|Appears in Collections:||分子醫學研究所|
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