GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif

Shewan, A. M., van Dam, E. M., Martin, S., Luen, T. B., Hong, W. J., Bryant, N. J. and James, D. E. (2003) GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif. Molecular Biology of The Cell, 14 3: 973-986. doi:10.1091/mbc.E02-06-0315

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Author Shewan, A. M.
van Dam, E. M.
Martin, S.
Luen, T. B.
Hong, W. J.
Bryant, N. J.
James, D. E.
Title GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2003-03
Sub-type Article (original research)
DOI 10.1091/mbc.E02-06-0315
Open Access Status File (Publisher version)
Volume 14
Issue 3
Start page 973
End page 986
Total pages 14
Editor Botstein
David
Place of publication Bethesda, USA
Publisher American Society for Cell Biology
Collection year 2003
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780105 Biological sciences
Abstract Insulin stimulates glucose transport in fat and muscle cells by triggering exocytosis of the glucose transporter GLUT4. To define the intracellular trafficking of GLUT4, we have studied the internalization of an epitope-tagged version of GLUT4 from the cell surface. GLUT4 rapidly traversed the endosomal system en route to a perinuclear location. This perinuclear GLUT4 compartment did not colocalize with endosomal markers (endosomal antigen I protein, transferrin) or TGN38, but showed significant overlap with the TGN target (t)-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) Syntaxins 6 and 16. These results were confirmed by vesicle immunoisolation. Consistent with a role for Syntaxins 6 and 16 in GLUT4 trafficking we found that their expression was up-regulated significantly during adipocyte differentiation and insulin stimulated their movement to the cell surface. GLUT4 trafficking between endosomes and trans-Golgi network was regulated via an acidic targeting motif in the carboxy terminus of GLUT4, because a mutant lacking this motif was retained in endosomes. We conclude that GLUT4 is rapidly transported from the cell surface to a subdomain of the trans-Golgi network that is enriched in the t-SNAREs Syntaxins 6 and 16 and that an acidic targeting motif in the C-terminal tail of GLUT4 plays an important role in this process.
Keyword Cell Biology
Glucose-transporter Glut4
Immature Secretory Granules
3t3-l1 Adipocytes
Plasma-membrane
Early/recycling Endosomes
Internalization Motif
Transferrin Receptor
Regulated Transport
Skeletal-muscle
Cell-surface
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 01:22:20 EST