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J. Biol. Chem., Vol. 277, Issue 50, 47972-47975, December 13, 2002
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From the Boston University School of Medicine,
Boston, Massachusetts 02118
Insulin stimulates translocation of the glucose
transporter isoform 4 (Glut4) from an intracellular storage compartment
to the plasma membrane in fat and skeletal muscle cells. At present, the nature of the Glut4 storage compartment is unclear. According to
one model, this compartment represents a population of preformed small
vesicles that fuse with the plasma membrane in response to insulin
stimulation. Alternatively, Glut4 may be retained in large donor
membranes, and insulin stimulates the formation of transport vesicles
that deliver Glut4 to the cell surface. Finally, insulin can induce
plasma membrane fusion of the preformed vesicles and, also, stimulate
the formation of new vesicles. In extracts of fat and skeletal muscle
cells, Glut4 is predominantly found in small insulin-sensitive 60-70 S
membrane vesicles that may or may not artificially derive from large
donor membranes during cell homogenization. Here, we use a cell-free
reconstitution assay to demonstrate that small Glut4-containing
vesicles are formed from large rapidly sedimenting donor membranes in a
cytosol-, ATP-, time-, and temperature-dependent fashion
and, therefore, do not represent an artifact of homogenization. Thus,
small insulin-responsive vesicles represent the major form of Glut4
storage in the living adipose cell. Fusion of these vesicles with
the plasma membrane may be largely responsible for the primary effect
of insulin on glucose transport in fat tissue. In addition, our results
suggest that insulin may also stimulate the formation of Glut4 vesicles and accelerate Glut4 recycling to the plasma membrane.
ACCELERATED PUBLICATION
Translocation of Small Preformed Vesicles Is Responsible for the
Insulin Activation of Glucose Transport in Adipose Cells
EVIDENCE FROM THE IN VITRO RECONSTITUTION
ASSAY*
*
This work was supported by research Grants DK52057 and
DK56736 from the National Institutes of Health and by a research grant from the American Diabetes Association (to K. V. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Boston University
School of Medicine, Dept. of Biochemistry, K124D, 715 Albany St.,
Boston, MA 02118. Tel.: 617-638-5049; Fax: 617-638-5339; E-mail:
kandror@biochem.bumc.bu.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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