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Sortilin and retromer mediate retrograde transport of Glut4 in 3T3-L1 adipocytes

Pan, Xiang, Zaarur, Nava, Singh, Maneet, Morin, Peter, Kandror, Konstantin V.·2017·Molecular Biology of the Cell
DOI 10.1091/mbc.e16-11-0777PMC PMC5469609
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Abstract

Sortilin is a multiligand sorting receptor responsible for the anterograde transport of lysosomal enzymes and substrates. Here we demonstrate that sortilin is also involved in retrograde protein traffic. In cultured 3T3-L1 adipocytes, sortilin together with retromer rescues Glut4 from degradation in lysosomes and retrieves it to the TGN, where insulin-­responsive vesicles are formed. Mechanistically, the luminal Vps10p domain of sortilin interacts with the first luminal loop of Glut4, and the cytoplasmic tail of sortilin binds to retromer. Ablation of the retromer does not affect insulin signaling but decreases the stability of sortilin and Glut4 and blocks their entry into the small vesicular carriers. As a result, Glut4 cannot reach the insulin-responsive compartment, and insulin-stimulated glucose uptake in adipocytes is suppressed. We suggest that sortilin- and retromer-mediated Glut4 retrieval from endosomes may represent a step in the Glut4 pathway vulnerable to the development of insulin resistance and diabetes.

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Metadata

Authors
Pan, X., Zaarur, N., Singh, M., Morin, P., & Kandror, K. V.
Affiliations
  • Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118
  • Edith Nourse Rogers Memorial Veterans Hospital, Bedford, MA 01730
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2017-06-15
Volume
28
Issue
12
Pages
1667-1675
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e16-11-0777
PMC
PMC5469609
Cited by
89
References
2
Language
en

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