Regulation of osteoclast differentiation and actin ring formation by the cytolinker protein plectin

Takuma Matsubara, Masayuki Kinbara, Toshihiro Maeda, Mitsuhiro Yoshizawa, Shoichiro Kokabu, Teruko Yamamoto

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)


Osteoclasts are cells that resorb the bone matrix and maintain bone and calcium homeostasis. An actin ring is a characteristic actin structure that is essential for bone resorption by osteoclasts. Tyrosine kinase Src deficient osteoclasts do not form actin rings; thus, Src is a key molecule for actin ring formation in osteoclasts. However, how Src regulates actin ring formation is not fully understood. We identified the cytolinker protein plectin as a Src-binding protein by immunoprecipitation and liquid chromatography tandem mass spectrometry. Plectin is a huge protein (>500 kDa) and regulates the cytoskeleton by binding to actin and tubulin. We assessed the expression and role of plectin in osteoclasts. Plectin was expressed and co-localized with Src close to the actin ring in osteoclasts. Moreover, plectin was tyrosine-phosphorylated by Src. Differentiation and actin ring formation were inhibited by downregulation of plectin. These results suggest an important role for plectin in osteoclast differentiation and actin ring formation through Src binding.

Original languageEnglish
Pages (from-to)472-476
Number of pages5
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2017 Aug 5


  • Actin organization
  • Osteoclast
  • Plectin
  • Src

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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