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J Biol Chem, Vol. 273, Issue 31, 19740-19746, July 31, 1998
From the Second Department of Internal Medicine, Kobe University
School of Medicine, 7-5-1 Kusunoki-cho,
Chuo-ku, Kobe 650, Japan
Insulin induces the translocation of vesicles
containing the glucose transporter GLUT4 from an intracellular
compartment to the plasma membrane in adipocytes. SNARE proteins have
been implicated in the docking and fusion of these vesicles with the
cell membrane. The role of Munc18c, previously identified as an
n-Sec1/Munc18 homolog in 3T3-L1 adipocytes, in insulin-regulated GLUT4
trafficking has now been investigated in 3T3-L1 adipocytes. In these
cells, Munc18c was predominantly associated with syntaxin4, although it
bound both syntaxin2 and syntaxin4 to similar extents in
vitro. In addition, SNAP-23, an adipocyte homolog of SNAP-25,
associated with both syntaxins 2 and 4 in 3T3-L1 adipocytes.
Overexpression of Munc18c in 3T3-L1 adipocytes by adenovirus-mediated
gene transfer resulted in inhibition of insulin-stimulated glucose
transport in a virus dose-dependent manner (maximal effect,
~50%) as well as in inhibition of sorbitol-induced glucose transport
(by ~35%), which is mediated by a pathway different from that used
by insulin. In contrast, Munc18b, which is also expressed in adipocytes
but which did not bind to syntaxin4, had no effect on glucose
transport. Furthermore, overexpression of Munc18c resulted in
inhibition of insulin-induced translocation of GLUT4, but not of that
of GLUT1, to the plasma membrane. These results suggest that Munc18c is
involved in the insulin-dependent trafficking of GLUT4 from the intracellular storage compartment to the plasma membrane in 3T3-L1
adipocytes by modulating the formation of a SNARE complex that includes
syntaxin4.
Inhibition of Insulin-induced GLUT4 Translocation by Munc18c
through Interaction with Syntaxin4 in 3T3-L1 Adipocytes
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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