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FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans

Insulin signaling plays a central role in the regulation of facilitative glucose transporters (GLUTs) in humans. To establish Caenorhabditis elegans (C. elegans) as a model to study the mechanism underlying insulin regulation of GLUT, we identified that FGT‐1 is most likely the only functional GLUT...

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Detalles Bibliográficos
Autores principales: Kitaoka, Shun, Morielli, Anthony D., Zhao, Feng‐Qi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4887973/
https://www.ncbi.nlm.nih.gov/pubmed/27419060
http://dx.doi.org/10.1002/2211-5463.12068
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author Kitaoka, Shun
Morielli, Anthony D.
Zhao, Feng‐Qi
author_facet Kitaoka, Shun
Morielli, Anthony D.
Zhao, Feng‐Qi
author_sort Kitaoka, Shun
collection PubMed
description Insulin signaling plays a central role in the regulation of facilitative glucose transporters (GLUTs) in humans. To establish Caenorhabditis elegans (C. elegans) as a model to study the mechanism underlying insulin regulation of GLUT, we identified that FGT‐1 is most likely the only functional GLUT homolog in C. elegans and is ubiquitously expressed. The FGT‐1‐mediated glucose uptake was almost completely defective in insulin/IGF‐like signaling (IIS) mutants daf‐2 and age‐1, and this defect mainly resulted from the down‐regulated FGT‐1 protein expression. However, glycosylation may also be involved because OGA‐1, an O‐GlcNAcase, was essential for the function of FGT‐1. Thus, our study showed that C. elegans can be a new powerful model system to study insulin regulation of GLUT.
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spelling pubmed-48879732016-07-14 FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans Kitaoka, Shun Morielli, Anthony D. Zhao, Feng‐Qi FEBS Open Bio Research Articles Insulin signaling plays a central role in the regulation of facilitative glucose transporters (GLUTs) in humans. To establish Caenorhabditis elegans (C. elegans) as a model to study the mechanism underlying insulin regulation of GLUT, we identified that FGT‐1 is most likely the only functional GLUT homolog in C. elegans and is ubiquitously expressed. The FGT‐1‐mediated glucose uptake was almost completely defective in insulin/IGF‐like signaling (IIS) mutants daf‐2 and age‐1, and this defect mainly resulted from the down‐regulated FGT‐1 protein expression. However, glycosylation may also be involved because OGA‐1, an O‐GlcNAcase, was essential for the function of FGT‐1. Thus, our study showed that C. elegans can be a new powerful model system to study insulin regulation of GLUT. John Wiley and Sons Inc. 2016-04-21 /pmc/articles/PMC4887973/ /pubmed/27419060 http://dx.doi.org/10.1002/2211-5463.12068 Text en © 2016 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Kitaoka, Shun
Morielli, Anthony D.
Zhao, Feng‐Qi
FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title_full FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title_fullStr FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title_full_unstemmed FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title_short FGT‐1‐mediated glucose uptake is defective in insulin/IGF‐like signaling mutants in Caenorhabditis elegans
title_sort fgt‐1‐mediated glucose uptake is defective in insulin/igf‐like signaling mutants in caenorhabditis elegans
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4887973/
https://www.ncbi.nlm.nih.gov/pubmed/27419060
http://dx.doi.org/10.1002/2211-5463.12068
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