2019年3月
Tks5 and Dynamin-2 enhance actin bundle rigidity in invadosomes to promote myoblast fusion
The Journal of cell biology
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- 巻
- 218
- 号
- 5
- 開始ページ
- 1670
- 終了ページ
- 1685
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1083/jcb.201809161
- 出版者・発行元
- ROCKEFELLER UNIV PRESS
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.
- リンク情報
- ID情報
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- DOI : 10.1083/jcb.201809161
- ISSN : 0021-9525