Tks5 and dynamin-2 enhance actin bundle rigidity in invadosomes to promote myoblast fusion

Mei Chun Chuang, Shan Shan Lin, Ryosuke L. Ohniwa, Gang Hui Lee, You An Su, Yu Chen Chang, Ming Jer Tang, Ya Wen Liu

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1670-1685
Number of pages16
JournalJournal of Cell Biology
Issue number5
Publication statusPublished - 2019 May 1

All Science Journal Classification (ASJC) codes

  • Cell Biology


Dive into the research topics of 'Tks5 and dynamin-2 enhance actin bundle rigidity in invadosomes to promote myoblast fusion'. Together they form a unique fingerprint.

Cite this