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Related Experiment Videos

Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation.

Hiroyuki Sano1, Susan Kane, Eiko Sano

  • 1Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.

Biochemical and Biophysical Research Communications
|May 26, 2005
PubMed
Summary

Phosphorylation of the Synip protein on serine 99 is not required for insulin-stimulated glucose transporter type 4 (GLUT4) translocation. This finding challenges previous proposals linking Synip phosphorylation to GLUT4 trafficking in adipocytes.

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Area of Science:

  • Cell biology
  • Molecular signaling
  • Metabolic regulation

Background:

  • Insulin rapidly stimulates glucose transporter type 4 (GLUT4) translocation to the plasma membrane in adipocytes and muscle cells.
  • This process is largely mediated by the insulin-activated protein kinase Akt.
  • Synphilin interacting protein (Synip) is a potential Akt substrate involved in regulating GLUT4 trafficking, associating with syntaxin4.

Purpose of the Study:

  • To investigate the role of Synip phosphorylation at serine 99 in insulin-stimulated GLUT4 translocation.
  • To determine if Akt-mediated phosphorylation of Synip on serine 99 is essential for GLUT4 trafficking.

Main Methods:

  • Utilized 3T3-L1 adipocytes for experimental studies.
  • Employed a Synip mutant (S99A) lacking the serine 99 phosphorylation site.

Related Experiment Videos

  • Assessed the effect of Synip S99A mutant overexpression on insulin-stimulated GLUT4 translocation.

    • Main Results:

    • Overexpression of the Synip S99A mutant did not impede insulin-stimulated GLUT4 translocation.
    • This indicates that the serine 99 phosphorylation site on Synip is not critical for the trafficking process.

    Conclusions:

    • Phosphorylation of Synip on serine 99 is not a prerequisite for insulin-induced GLUT4 translocation.
    • The proposed mechanism where Synip phosphorylation enables GLUT4 translocation by dissociating from syntaxin4 is not supported by these findings.