@article{oai:tsukuba.repo.nii.ac.jp:00051973,
 author = {大庭, 良介 and OHNIWA, Ryosuke and Chuang, Mei-Chun and Lin, Shan-Shan and Lee, Gang-Hui and Su, You-An and Chang, Yu-Chen and Tang, Ming-Jer and Liu, Ya-Wen},
 issue = {5},
 journal = {The journal of cell biology},
 month = {Mar},
 note = {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.},
 pages = {1670--1685},
 title = {Tks5 and Dynamin-2 enhance actin bundle rigidity in invadosomes to promote myoblast fusion},
 volume = {218},
 year = {2019},
 yomi = {オオニワ, リョウスケ}
}