Myosin IIA participates in docking of Glut4 storage vesicles with the plasma membrane in 3T3-L1 adipocytes

Le Thi Kim Chung, Toshio Hosaka, Nagakatsu Harada, Bayasgalan Jambaldorj, Keiko Fukunaga, Yuka Nishiwaki, Kiyoshi Teshigawara, Tohru Sakai, Yutaka Nakaya, Makoto Funaki

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


In adipocytes and myocytes, insulin stimulation translocates glucose transporter 4 (Glut4) storage vesicles (GSVs) from their intracellular storage sites to the plasma membrane (PM) where they dock with the PM. Then, Glut4 is inserted into the PM and initiates glucose uptake into these cells. Previous studies using chemical inhibitors demonstrated that myosin II participates in fusion of GSVs and the PM and increase in the intrinsic activity of Glut4. In this study, the effect of myosin IIA on GSV trafficking was examined by knocking down myosin IIA expression. Myosin IIA knockdown decreased both glucose uptake and exposures of myc-tagged Glut4 to the cell surface in insulin-stimulated cells, but did not affect insulin signal transduction. Interestingly, myosin IIA knockdown failed to decrease insulin-dependent trafficking of Glut4 to the PM. Moreover, in myosin IIA knockdown cells, insulin-stimulated binding of GSV SNARE protein, vesicle-associated membrane protein 2 (VAMP2) to PM SNARE protein, syntaxin 4 was inhibited. These data suggest that myosin IIA plays a role in insulin-stimulated docking of GSVs to the PM in 3T3-L1 adipocytes through SNARE complex formation.

Original languageEnglish
Pages (from-to)995-999
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Jan 1 2010
Externally publishedYes


  • Glut4
  • Myosin IIA
  • Syntaxin 4
  • VAMP2

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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