Essential roles of snap-29 in C. elegans

Dev Biol. 2011 Jul 1;355(1):77-88. doi: 10.1016/j.ydbio.2011.04.013. Epub 2011 Apr 22.

Abstract

SNARE domain proteins are key molecules mediating intracellular fusion events. SNAP25 family proteins are unique target-SNAREs possessing two SNARE domains. Here we report the genetic, molecular, and cell biological characterization of C. elegans SNAP-29. We found that snap-29 is an essential gene required throughout the life-cycle. Depletion of snap-29 by RNAi in adults results in sterility associated with endomitotic oocytes and pre-meiotic maturation of the oocytes. Many of the embryos that are produced are multinucleated, indicating a defect in embryonic cytokinesis. A profound defect in secretion by oocytes and early embryos in animals lacking SNAP-29 appears to be the underlying defect connecting these phenotypes. Further analysis revealed defects in basolateral and apical secretion by intestinal epithelial cells in animals lacking SNAP-29, indicating a broad requirement for this protein in the secretory pathway. A SNAP-29-GFP fusion protein was enriched on recycling endosomes, and loss of SNAP-29 disrupted recycling endosome morphology. Taken together these results suggest a requirement for SNAP-29 in the fusion of post-Golgi vesicles with the recycling endosome for cargo to reach the cell surface.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / physiology*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Caenorhabditis elegans Proteins / physiology*
  • Endosomes / physiology*
  • Female
  • Golgi Apparatus / physiology*
  • Infertility / genetics*
  • Male
  • Oocytes / metabolism
  • Oocytes / physiology
  • Q-SNARE Proteins / genetics
  • Q-SNARE Proteins / metabolism
  • Q-SNARE Proteins / physiology*
  • RNA Interference
  • SNARE Proteins / genetics
  • SNARE Proteins / metabolism
  • SNARE Proteins / physiology*

Substances

  • Caenorhabditis elegans Proteins
  • Q-SNARE Proteins
  • SNAP-29 protein, C elegans
  • SNARE Proteins