Regulation of presynaptic terminal organization by C. elegans RPM-1, a putative guanine nucleotide exchanger with a RING-H2 finger domain

Neuron. 2000 May;26(2):331-43. doi: 10.1016/s0896-6273(00)81167-8.


Presynaptic terminals contain highly organized subcellular structures to facilitate neurotransmitter release. In C. elegans, the typical presynaptic terminal has an electron-dense active zone surrounded by synaptic vesicles. Loss-of-function mutations in the rpm-1 gene result in abnormally structured presynaptic terminals in GABAergic neuromuscular junctions (NMJs), most often manifested as a single presynaptic terminal containing multiple active zones. The RPM-1 protein has an RCC1-like guanine nucleotide exchange factor (GEF) domain and a RING-H2 finger. RPM-1 is most similar to the Drosophila presynaptic protein Highwire (HIW) and the mammalian Myc binding protein Pam. RPM-1 is localized to the presynaptic region independent of synaptic vesicles and functions cell autonomously. The temperature-sensitive period of rpm-1 coincides with the time of synaptogenesis. rpm-1 may regulate the spatial arrangement, or restrict the formation, of presynaptic structures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Amino Acid Sequence
  • Animals
  • Biomarkers
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins*
  • Carrier Proteins / genetics
  • Drosophila / metabolism
  • Drosophila Proteins*
  • Green Fluorescent Proteins
  • Guanine Nucleotide Exchange Factors / genetics
  • Guanine Nucleotide Exchange Factors / physiology*
  • Indicators and Reagents / pharmacokinetics
  • Luminescent Proteins / pharmacokinetics
  • Mixed Function Oxygenases*
  • Molecular Sequence Data
  • Mutation / genetics
  • Mutation / physiology
  • Nerve Tissue Proteins / genetics
  • Neurons / physiology
  • Presynaptic Terminals / metabolism
  • Presynaptic Terminals / physiology*
  • Receptors, GABA / metabolism
  • Synapses / metabolism
  • Synapses / physiology
  • Synaptic Vesicles / metabolism
  • Synaptic Vesicles / ultrastructure
  • Tissue Distribution
  • Ubiquitin-Protein Ligases
  • Zinc Fingers / genetics


  • Adaptor Proteins, Signal Transducing
  • Biomarkers
  • Caenorhabditis elegans Proteins
  • Carrier Proteins
  • Drosophila Proteins
  • Guanine Nucleotide Exchange Factors
  • HIW protein, Drosophila
  • Indicators and Reagents
  • Luminescent Proteins
  • Nerve Tissue Proteins
  • RPM-1 protein, C elegans
  • Receptors, GABA
  • Green Fluorescent Proteins
  • Mixed Function Oxygenases
  • MYCBP2 protein, human
  • Ubiquitin-Protein Ligases