Glycogen synthase kinase-3 and Axin function in a beta-catenin-independent pathway that regulates neurite outgrowth in neuroblastoma cells

Mol Cell Neurosci. 2003 Nov;24(3):673-86. doi: 10.1016/s1044-7431(03)00229-x.

Abstract

We have sought to determine the roles of beta-catenin and the Wnt signaling pathway in neurite outgrowth using a model cell system, the Neuro-2a neuroblastoma cell line. Activation of the Wnt signaling pathway disrupts a multiprotein complex that includes beta-catenin, Axin, and glycogen synthase kinase-3 (GSK-3), which would otherwise promote the phosphorylation and degradation of beta-catenin. Stabilized beta-catenin accumulates in the cytosol and in the nucleus; in the nucleus it binds to TCF family transcription factors, forming a bipartite transcriptional activator of Wnt target genes. These events can be mimicked by lithium (Li(+)), which inhibits GSK-3 activity. Both Li(+) and the GSK-3 inhibitor SB415286 induced neurite outgrowth of Neuro-2a cells. Li(+)-induced neurite outgrowth did not require beta-catenin-/TCF-dependent transcription, and increasing levels of beta-catenin either by transfection or using Wnt-3A was not sufficient to induce neurite outgrowth. Interestingly, Axin, which is also a substrate for GSK-3, was destabilized by Li(+) and ectopic expression of Axin inhibited Li(+)-induced neurite outgrowth. Deletion analysis of Axin indicated that this inhibition required the GSK-3 binding site, but not the beta-catenin binding site. Our results suggest that a signaling pathway involving Axin and GSK-3, but not beta-catenin, regulates Li(+)-induced neurite outgrowth in Neuro-2a cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Axin Protein
  • Binding Sites / physiology
  • Cell Differentiation / drug effects
  • Cell Differentiation / physiology*
  • Cell Nucleus / metabolism
  • Culture Media, Conditioned / pharmacology
  • Cytoskeletal Proteins / metabolism
  • Cytosol / metabolism
  • Enzyme Inhibitors / pharmacology
  • Gene Deletion
  • Glycogen Synthase Kinase 3 / antagonists & inhibitors
  • Glycogen Synthase Kinase 3 / metabolism*
  • Lithium / pharmacology
  • Macromolecular Substances
  • Mice
  • Models, Biological
  • Multiprotein Complexes
  • Neurites / drug effects
  • Neurites / metabolism*
  • Neurites / ultrastructure
  • Neuroblastoma / metabolism
  • Proto-Oncogene Proteins / metabolism*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Trans-Activators / metabolism
  • Transcription Factors / drug effects
  • Transcription Factors / physiology
  • Transcriptional Activation / physiology
  • Tumor Cells, Cultured
  • Wnt Proteins
  • Zebrafish Proteins*
  • beta Catenin

Substances

  • Axin Protein
  • CTNNB1 protein, mouse
  • Culture Media, Conditioned
  • Cytoskeletal Proteins
  • Enzyme Inhibitors
  • Macromolecular Substances
  • Multiprotein Complexes
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • Trans-Activators
  • Transcription Factors
  • Wnt Proteins
  • Zebrafish Proteins
  • beta Catenin
  • Lithium
  • Glycogen Synthase Kinase 3