RIC-7 promotes neuropeptide secretion

PLoS Genet. 2012 Jan;8(1):e1002464. doi: 10.1371/journal.pgen.1002464. Epub 2012 Jan 19.

Abstract

Secretion of neurotransmitters and neuropeptides is mediated by exocytosis of distinct secretory organelles, synaptic vesicles (SVs) and dense core vesicles (DCVs) respectively. Relatively little is known about factors that differentially regulate SV and DCV secretion. Here we identify a novel protein RIC-7 that is required for neuropeptide secretion in Caenorhabditis elegans. The RIC-7 protein is expressed in all neurons and is localized to presynaptic terminals. Imaging, electrophysiology, and behavioral analysis of ric-7 mutants indicates that acetylcholine release occurs normally, while neuropeptide release is significantly decreased. These results suggest that RIC-7 promotes DCV-mediated secretion.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylcholine / metabolism
  • Aldicarb
  • Animals
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Diacylglycerol Kinase / genetics
  • Diacylglycerol Kinase / metabolism
  • Drug Hypersensitivity / genetics
  • Exocytosis
  • Muscle, Skeletal / drug effects
  • Mutation
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Neurons / cytology
  • Neurons / metabolism*
  • Neuropeptides / genetics*
  • Neuropeptides / metabolism*
  • Presynaptic Terminals / metabolism*
  • Secretory Vesicles / genetics
  • Secretory Vesicles / metabolism
  • Synaptic Vesicles / genetics
  • Synaptic Vesicles / metabolism
  • gamma-Aminobutyric Acid / pharmacology

Substances

  • Caenorhabditis elegans Proteins
  • Nerve Tissue Proteins
  • Neuropeptides
  • Ric-7 protein, C elegans
  • gamma-Aminobutyric Acid
  • Aldicarb
  • Diacylglycerol Kinase
  • Acetylcholine