title: Diapause is associated with a change in the polarity of secretion of insulin-like peptides.
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.
authors.affiliation: Department of Bioresources Science, The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi, Tottori 680-8553, Japan.
authors.forename: Yohei
authors.initials: Y
authors.lastname: Matsunaga
authors.affiliation: Section for Genomics for Longevity and Health, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan.
authors.forename: Yoko
authors.initials: Y
authors.lastname: Honda
authors.affiliation: Section for Genomics for Longevity and Health, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan.
authors.forename: Shuji
authors.initials: S
authors.lastname: Honda
authors.affiliation: Department of Bioresources Science, The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi, Tottori 680-8553, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Iwasaki
authors.affiliation: Department of Pathology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Qadota
authors.affiliation: Department of Pathology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
authors.forename: Guy M
authors.initials: GM
authors.lastname: Benian
authors.affiliation: Department of Bioresources Science, The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi, Tottori 680-8553, Japan.
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Kawano
mesh_terms: D000818:Animals; D015153:Blotting, Western; D017173:Caenorhabditis elegans / Q000235:genetics*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics* / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000378:metabolism; D016764:Cell Polarity; D004847:Epithelial Cells / Q000378:metabolism*; D048788:Growth and Development / Q000235:genetics*; D061385:Insulins; D007413:Intestinal Mucosa / Q000166:cytology / Q000378:metabolism*; D007814:Larva; D008018:Life Cycle Stages; D008856:Microscopy, Fluorescence; D036361:Peptide Hormones / Q000235:genetics / Q000378:metabolism; D011972:Receptor, Insulin / Q000235:genetics / Q000378:metabolism; D013002:Somatomedins / Q000235:genetics* / Q000378:metabolism
chemical_list: D029742:Caenorhabditis elegans Proteins; C525653:Ins-7 protein, C elegans; D061385:Insulins; D036361:Peptide Hormones; D013002:Somatomedins; C473608:daf-28 protein, C elegans; D011972:Receptor, Insulin; D002265:Carboxylic Ester Hydrolases; C095990:ges-1 protein, C elegans
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