Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes

Insulin stimulates the movement of glucose transporter-4 (Glut4)–containing vesicles to the plasma membrane of adipose cells. We investigated the role of post-Golgi t-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in the trafficking of Glut4 in 3T3-L1 adipocytes. Gre...

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Auteurs principaux: Perera, H. Kumudu I., Clarke, Mairi, Morris, Nicholas J., Hong, Wanjin, Chamberlain, Luke H., Gould, Gwyn W.
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Publié: The American Society for Cell Biology 2003
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Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC165689/
https://ncbi.nlm.nih.gov/pubmed/12857877
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1091/mbc.E02-11-0722
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spelling pubmed-1656892003-11-13 Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes Perera, H. Kumudu I. Clarke, Mairi Morris, Nicholas J. Hong, Wanjin Chamberlain, Luke H. Gould, Gwyn W. Mol Biol Cell Articles Insulin stimulates the movement of glucose transporter-4 (Glut4)–containing vesicles to the plasma membrane of adipose cells. We investigated the role of post-Golgi t-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in the trafficking of Glut4 in 3T3-L1 adipocytes. Greater than 85% of syntaxin 6 was found in Glut4-containing vesicles, and this t-SNARE exhibited insulin-stimulated movement to the plasma membrane. In contrast, the colocalization of Glut4 with syntaxin 7, 8, or 12/13 was limited and these molecules did not translocate to the plasma membrane. We used adenovirus to overexpress the cytosolic domain of these syntaxin's and studied their effects on Glut4 traffic. Overexpression of the cytosolic domain of syntaxin 6 did not affect insulin-stimulated glucose transport, but increased basal deGlc transport and cell surface Glut4 levels. Moreover, the syntaxin 6 cytosolic domain significantly reduced the rate of Glut4 reinternalization after insulin withdrawal and perturbed subendosomal Glut4 sorting; the corresponding domains of syntaxins 8 and 12 were without effect. Our data suggest that syntaxin 6 is involved in a membrane-trafficking step that sequesters Glut4 away from traffic destined for the plasma membrane. We speculate that this is at the level of traffic of Glut4 into its unique storage compartment and that syntaxin 16 may be involved. The American Society for Cell Biology 2003-07 /pmc/articles/PMC165689/ /pubmed/12857877 http://dx.doi.org/10.1091/mbc.E02-11-0722 Text en Copyright © 2003, The American Society for Cell Biology
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Articles
spellingShingle Articles
Perera, H. Kumudu I.
Clarke, Mairi
Morris, Nicholas J.
Hong, Wanjin
Chamberlain, Luke H.
Gould, Gwyn W.
Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
description Insulin stimulates the movement of glucose transporter-4 (Glut4)–containing vesicles to the plasma membrane of adipose cells. We investigated the role of post-Golgi t-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) in the trafficking of Glut4 in 3T3-L1 adipocytes. Greater than 85% of syntaxin 6 was found in Glut4-containing vesicles, and this t-SNARE exhibited insulin-stimulated movement to the plasma membrane. In contrast, the colocalization of Glut4 with syntaxin 7, 8, or 12/13 was limited and these molecules did not translocate to the plasma membrane. We used adenovirus to overexpress the cytosolic domain of these syntaxin's and studied their effects on Glut4 traffic. Overexpression of the cytosolic domain of syntaxin 6 did not affect insulin-stimulated glucose transport, but increased basal deGlc transport and cell surface Glut4 levels. Moreover, the syntaxin 6 cytosolic domain significantly reduced the rate of Glut4 reinternalization after insulin withdrawal and perturbed subendosomal Glut4 sorting; the corresponding domains of syntaxins 8 and 12 were without effect. Our data suggest that syntaxin 6 is involved in a membrane-trafficking step that sequesters Glut4 away from traffic destined for the plasma membrane. We speculate that this is at the level of traffic of Glut4 into its unique storage compartment and that syntaxin 16 may be involved.
author Perera, H. Kumudu I.
Clarke, Mairi
Morris, Nicholas J.
Hong, Wanjin
Chamberlain, Luke H.
Gould, Gwyn W.
author_facet Perera, H. Kumudu I.
Clarke, Mairi
Morris, Nicholas J.
Hong, Wanjin
Chamberlain, Luke H.
Gould, Gwyn W.
author_sort Perera, H. Kumudu I.
title Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
title_short Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
title_full Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
title_fullStr Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
title_full_unstemmed Syntaxin 6 Regulates Glut4 Trafficking in 3T3-L1 Adipocytes
title_sort syntaxin 6 regulates glut4 trafficking in 3t3-l1 adipocytes
publisher The American Society for Cell Biology
publisher_facet The American Society for Cell Biology
publishDate 2003
url https://ncbi.nlm.nih.gov/pmc/articles/PMC165689/
https://ncbi.nlm.nih.gov/pubmed/12857877
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1091/mbc.E02-11-0722
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