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RAE-1, a novel PHR binding protein, is required for axon termination and synapse formation in Caenorhabditis elegans

Academic Article
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Overview

authors

  • Grill, Brock
  • Chen, L. Z.
  • Tulgren, E. D.
  • Baker, S. T.
  • Bienvenut, W.
  • Anderson, M.
  • Quadroni, M.
  • Jin, Y. S.
  • Garner, C. C.

publication date

  • February 2012

journal

  • Journal of Neuroscience  Journal

abstract

  • Previous studies in Caenorhabditis elegans showed that RPM-1 (Regulator of Presynaptic Morphology-1) regulates axon termination and synapse formation. To understand the mechanism of how rpm-1 functions, we have used mass spectrometry to identify RPM-1 binding proteins, and have identified RAE-1 (RNA Export protein-1) as an evolutionarily conserved binding partner. We define a RAE-1 binding region in RPM-1, and show that this binding interaction is conserved and also occurs between Rae1 and the human ortholog of RPM-1 called Pam (protein associated with Myc). rae-1 loss of function causes similar axon and synapse defects, and synergizes genetically with two other RPM-1 binding proteins, GLO-4 and FSN-1. Further, we show that RAE-1 colocalizes with RPM-1 in neurons, and that rae-1 functions downstream of rpm-1. These studies establish a novel postmitotic function for rae-1 in neuronal development.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified
  • Axons
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins
  • F-Box Proteins
  • Gene Expression Regulation
  • Guanine Nucleotide Exchange Factors
  • Humans
  • Immunoprecipitation
  • Luminescent Proteins
  • Mass Spectrometry
  • Mechanoreceptors
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Mutation
  • Nuclear Matrix-Associated Proteins
  • Nucleocytoplasmic Transport Proteins
  • Protein Binding
  • Signal Transduction
  • Synapses
  • Ubiquitin-Protein Ligases
  • rab GTP-Binding Proteins
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Identity

PubMed Central ID

  • PMC3302171

International Standard Serial Number (ISSN)

  • 0270-6474

Digital Object Identifier (DOI)

  • 10.1523/jneurosci.2901-11.2012

PubMed ID

  • 22357847
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Additional Document Info

start page

  • 2628

end page

  • 2636

volume

  • 32

issue

  • 8

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