Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33

Nature. 1995 Aug 10;376(6540):509-14. doi: 10.1038/376509a0.


Collapsin, a member of the newly recognized semaphorin family, contributes to axonal pathfinding during neural development by inhibiting growth cone extension. The mechanism of collapsin action is poorly understood. Here we use a Xenopus laevis oocyte expression system to identify molecules involved in collapsin signalling, because several experiments have raised the possibility that heterotrimeric GTP-binding proteins might participate in these events. A collapsin response mediator protein of relative molecular mass (M(r)) 62K (CRMP-62) required for collapsin-induced inward currents in X. laevis oocytes is isolated. CRMP-62 shares homology with UNC-33, a nematode neuronal protein required for appropriately directed axonal extension. CRMP-62 is localized exclusively in the developing chick nervous system. Introduction of anti-CRMP-62 antibodies into dorsal root ganglion neurons blocks collapsin-induced growth cone collapse. CRMP-62 appears to be an intracellular component of a signalling cascade initiated by an unidentified transmembrane collapsin-binding protein.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / physiology
  • Caenorhabditis elegans Proteins*
  • Cell Line
  • Cell Membrane / physiology
  • Chick Embryo
  • GTP-Binding Proteins / physiology
  • Ganglia, Spinal / physiology
  • Glycoproteins / physiology*
  • Helminth Proteins / physiology
  • Intercellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Nerve Growth Factors / physiology*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / immunology
  • Nerve Tissue Proteins / physiology*
  • Neurites / physiology
  • Neurons / physiology
  • Oocytes / drug effects
  • Oocytes / physiology
  • Recombinant Fusion Proteins / genetics
  • Semaphorin-3A
  • Signal Transduction
  • Virulence Factors, Bordetella / pharmacology
  • Xenopus laevis


  • Caenorhabditis elegans Proteins
  • Glycoproteins
  • Helminth Proteins
  • Intercellular Signaling Peptides and Proteins
  • Nerve Growth Factors
  • Nerve Tissue Proteins
  • Recombinant Fusion Proteins
  • Semaphorin-3A
  • Virulence Factors, Bordetella
  • collapsin response mediator protein-2
  • unc-33 protein, C elegans
  • GTP-Binding Proteins

Associated data

  • GENBANK/U17277
  • GENBANK/U17278
  • GENBANK/U17279