FGT-1 is The major glucose transporter in C. elegans and is central to aging pathways

Ying Feng, Barnabas G. Williams, Françoise Koumanov, Adrian J. Wolstenholme, G D Holman

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Caenorhabditis elegans is widely used as a model for investigation of the relationships between aging, nutrient restriction and signalling via the DAF-2 (abnormal dauer formation 2) receptor for insulin-like peptides and AGE-1 [ageing alteration 1; orthologue of PI3K (phosphoinositide 3-kinase)], but the identity of the glucose transporters that may link these processes is unknown. We unexpectedly find that of the eight putative GLUT (glucose transporter)-like genes only the two splice variants of one gene have a glucose transport function in an oocyte expression system. We have named this gene fgt-1 (facilitated glucose transporter, isoform 1). We show that knockdown of fgt-1 RNA leads to loss of glucose transport and reduced glucose metabolism in wild-type worms. The FGT-1 glucose transporters of C. elegans thus play a key role in glucose energy supply to C. elegans. Importantly, knockdown of fgt-1 leads to an extension of lifespan equivalent, but not additive, to that observed in daf-2 and age-1 mutant worms. The results of the present study are consistent with DAF-2 and AGE-1 signalling stimulating glucose transport in C. elegans and this process being associated with the longevity phenotype in daf-2 and age-1 mutant worms. We propose that fgt-1 constitutes a common axis for the lifespan extending effects of nutrient restriction and reduced insulin-like peptide signalling.
Original languageEnglish
Pages (from-to)219-229
Number of pages11
JournalBiochemical Journal
Volume456
Issue number2
DOIs
Publication statusPublished - 1 Dec 2013

Keywords

  • Aging
  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins
  • Cells, Cultured
  • Glucose
  • Glucose Transport Proteins, Facilitative
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Xenopus

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