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J Biol Chem, Vol. 274, Issue 40, 28087-28095, October 1, 1999
,,, and
From the An interaction of SNAP-23 and syntaxin 4 on the
plasma membrane with vesicle-associated synaptobrevin-2 and/or
cellubrevin, known as SNAP (soluble
N-ethyl-maleimide-sensitive factor attachment protein) receptors or SNAREs, has
been proposed to provide the targeting and/or fusion apparatus for
insulin-stimulated translocation of the GLUT4 isoform of glucose
transporter to the plasma membrane. By microinjecting 3T3-L1 adipocytes
with the Clostridium botulinum toxin B or E, which
proteolyzed synaptobrevin-2/cellubrevin and SNAP-23, respectively, we
investigated the role of these SNAREs in GLUT4, GLUT1, and transferrin
receptor trafficking. As expected, insulin stimulated the translocation
of GLUT4, GLUT1, and transferrin receptors to the plasma membrane. By
contrast, a constitutively active protein kinase B (PKB-DD) only
stimulated a translocation of GLUT4 and not GLUT1 or the transferrin
receptor. The GLUT4 response to PKB-DD was abolished by toxins B or E,
whereas the insulin-evoked translocation of GLUT4 was inhibited by
approximately 65%. These toxins had no significant effect on
insulin-stimulated transferrin receptor appearance at the cell surface.
Thus, insulin appears to induce GLUT4 translocation via two distinct
routes, only one of which involves SNAP-23 and
synaptobrevin-2/cellubrevin, and can be mobilized by PKB-DD. The PKB-,
SNAP-23-, and synaptobrevin-2/cellubrevin-independent GLUT4
translocation pathway may involve movement through recycling endosomes,
together with GLUT1 and transferrin receptors.
Department of Biochemistry, Imperial
College, London SW7 2AY and the § Department of
Biochemistry, School of Medical Sciences, University of Bristol,
Bristol, BS8 1TD United Kingdom
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