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J Biol Chem, Vol. 273, Issue 28, 17968-17977, July 10, 1998
From the In adipocytes, the insulin-regulated
aminopeptidase (IRAP) is trafficked through the same insulin-regulated
recycling pathway as the GLUT4 glucose transporter. We find that a
chimera, containing the cytoplasmic domain of IRAP fused to
transmembrane and extracellular domains of the transferrin receptor, is
slowly recycled and rapidly internalized in Chinese hamster ovary
cells. Morphological studies indicate that the chimera is slowly
trafficked through the general endosomal recycling compartment rather
than being sorted to a specialized recycling pathway. A chimera in
which a di-leucine sequence within the cytoplasmic domain of IRAP has
been mutated to alanines is rapidly internalized and rapidly recycled,
indicating that this di-leucine is required for the slow recycling but
not for the rapid internalization. Insulin stimulates a 2-3-fold
increase in the recycling of the chimera and only a 1.2-fold increase
in the recycling of the transferrin receptor. The effect of insulin on
the recycling of the chimera is blocked by wortmannin, a
phosphatidylinositol 3'-kinase inhibitor. GTP
Identification of an Insulin-responsive, Slow Endocytic Recycling
Mechanism in Chinese Hamster Ovary Cells
,,,,
Department of Biochemistry, Cornell
University Medical College, New York, New York 10021 and the
§ Department of Biochemistry, Dartmouth Medical School,
Hanover, New Hampshire 03755
S (guanosine
5'-3-O-(thio)triphosphate) increases the recycling of the
chimera by 50% but has no effect on the recycling of the transferrin
receptor. In these studies, we have identified in Chinese hamster ovary
cells a novel, slow endocytic recycling mechanism that is regulated by
insulin.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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