Diapause is associated with a change in the polarity of secretion of insulin-like peptides

Nat Commun. 2016 Feb 3:7:10573. doi: 10.1038/ncomms10573.

Abstract

The insulin/IGF-1 signalling (IIS) pathway plays an important role in the regulation of larval diapause, the long-lived growth arrest state called dauer arrest, in Caenorhabditis elegans. In this nematode, 40 insulin-like peptides (ILPs) have been identified as putative ligands of the IIS pathway; however, it remains unknown how ILPs modulate larval diapause. Here we show that the secretory polarity of INS-35 and INS-7, which suppress larval diapause, is changed in the intestinal epithelial cells at larval diapause. These ILPs are secreted from the intestine into the body cavity during larval stages. In contrast, they are secreted into the intestinal lumen and degraded during dauer arrest, only to be secreted into the body cavity again when the worms return to developmental growth. The process that determines the secretory polarity of INS-35 and INS-7, thus, has an important role in the modulation of larval diapause.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans Proteins / genetics*
  • Caenorhabditis elegans Proteins / metabolism
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism
  • Cell Polarity*
  • Epithelial Cells / metabolism*
  • Growth and Development / genetics*
  • Insulins
  • Intestinal Mucosa / cytology
  • Intestinal Mucosa / metabolism*
  • Larva
  • Life Cycle Stages
  • Microscopy, Fluorescence
  • Peptide Hormones / genetics
  • Peptide Hormones / metabolism
  • Receptor, Insulin / genetics
  • Receptor, Insulin / metabolism
  • Somatomedins / genetics*
  • Somatomedins / metabolism

Substances

  • Caenorhabditis elegans Proteins
  • Ins-7 protein, C elegans
  • Insulins
  • Peptide Hormones
  • Somatomedins
  • daf-28 protein, C elegans
  • Receptor, Insulin
  • Carboxylic Ester Hydrolases
  • ges-1 protein, C elegans