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Vol. 12, Issue 11, 3489-3501, November 2001
§ and
*Program in Physiology, Biophysics, and Molecular Medicine and
In several cell types, specific membrane proteins are retained
intracellularly and rapidly redistributed to the surface in response to
stimulation. In fat and muscle, the GLUT4 glucose transporter is
dynamically retained because it is rapidly internalized and slowly
recycled to the plasma membrane. Insulin increases the recycling of
GLUT4, resulting in a net translocation to the surface. We have shown
that fibroblasts also have an insulin-regulated recycling mechanism.
Here we show that GLUT4 is retained within the transferrin
receptor-containing general endosomal recycling compartment in Chinese
hamster ovary (CHO) cells rather than being segregated to a
specialized, GLUT4-recycling compartment. With the use of total
internal reflection microscopy, we demonstrate that the TR and GLUT4
are transported from the pericentriolar recycling compartment in
separate vesicles. These data provide the first functional evidence for
the formation of distinct classes of vesicles from the recycling
compartment. We propose that GLUT4 is dynamically retained within the
endosomal recycling compartment in CHO cells because it is concentrated
in vesicles that form more slowly than those that transport TR. In
3T3-L1 adipocytes, cells that naturally express GLUT4, we find that
GLUT4 is partially segregated to a separate compartment that is
inaccessible to the TR. We present a model for the formation of this
specialized compartment in fat cells, based on the general mechanism
described in CHO cells, which may explain the increased retention of
GLUT4 and its insulin-induced translocation in fat cells.
Department of Biochemistry, Weill Graduate School of
Medical Sciences of Cornell University, New York, New York 10021;
§Institute of Zellenlehre, University of Heidelberg,
Heidelberg, Germany D-69117; and Laboratory of
Cellular Biophysics, The Rockefeller University, New York, New York
10021
Corresponding author. E-mail address:
temcgraw{at}mail.med.cornell.edu.
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