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

Abstract

COLLAPSIN1, a member of the newly recognized semaphorin family2á¤-4, contributes to axonal pathfinding during neural development by inhibiting growth cone extension1á¤-5. 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 events6á¤-9. A collapsin response mediator protein of relative molecular mass (Mr) 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 extension10á¤-12. 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.

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Goshima, Y., Nakamura, F., Strittmatter, P. et al. Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature 376, 509–514 (1995). https://doi.org/10.1038/376509a0

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