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J Biol Chem. 1995 May 12;270(19):11489-95.

Dissection of GLUT4 recycling pathway into exocytosis and endocytosis in rat adipocytes. Evidence that GTP-binding proteins are involved in both processes.

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1
Department of Cell Biology, Gunma University, Maebashi, Japan.

Abstract

The effects of guanine nucleotides on either exocytosis or endocytosis of GLUT4 were examined in electrically permeabilized rat adipocytes by using Dk-(62-85), a major histocompatibility complex class I-derived peptide. Reversal of glucose transport activity that had been stimulated with insulin was completely blocked by Dk-(62-85). Likewise, endocytosis of the trypsin-cleaved 35-kDa fragment of GLUT4 was almost completely inhibited by the peptide. Insulin-stimulated glucose transport activity was enhanced about 50% by Dk-(62-85), whereas the basal transport activity was stimulated only slightly. Although guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) augmented glucose transport to the same extent as insulin in the absence of the peptide, glucose transport stimulated by GTP gamma S was only 60% of the insulin effect in the presence of the peptide; the effect of insulin was markedly enhanced by Dk-(62-85), whereas GTP gamma S-induced glucose transport was not affected, suggesting that GTP gamma S has an effect similar to that of the peptide. In fact, endocytosis of the 35-kDa fragment of GLUT4 was markedly inhibited by GTP gamma S. Additionally, GLUT4 endocytosis was accelerated by GTP but was inhibited by guanosine 5'-O-(2-thiodiphosphate). These results indicate that GTP gamma S induces translocation of GLUT4 by both stimulating exocytosis and inhibiting endocytosis. With respect to the dependence on GTP hydrolysis, distinct types of GTP-binding proteins are involved in exocytosis and endocytosis of GLUT4.

PMID:
7744788
DOI:
10.1074/jbc.270.19.11489
[Indexed for MEDLINE]
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