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

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  • Yohei Matsunaga

    (The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi
    Present address: Department of Pathology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.)

  • Yoko Honda

    (Section for Genomics for Longevity and Health, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku)

  • Shuji Honda

    (Section for Genomics for Longevity and Health, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku)

  • Takashi Iwasaki

    (The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi)

  • Hiroshi Qadota

    (Emory University School of Medicine, Atlanta)

  • Guy M. Benian

    (Emory University School of Medicine, Atlanta)

  • Tsuyoshi Kawano

    (The United Graduate School of Agricultural Sciences, Tottori University, Tottori-shi)

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.

Suggested Citation

  • Yohei Matsunaga & Yoko Honda & Shuji Honda & Takashi Iwasaki & Hiroshi Qadota & Guy M. Benian & Tsuyoshi Kawano, 2016. "Diapause is associated with a change in the polarity of secretion of insulin-like peptides," Nature Communications, Nature, vol. 7(1), pages 1-8, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10573
    DOI: 10.1038/ncomms10573
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