Depletion of casein kinase II by antisense oligonucleotide prevents neuritogenesis in neuroblastoma cells

EMBO J. 1993 Apr;12(4):1633-40.

Abstract

Casein kinase II is a multifunctional protein kinase which has been implicated in the regulation of cell growth and differentiation. This enzyme is much more abundant in neurons than in any other cell type. The treatment of neuroblastoma cells with an antisense oligodeoxyribonucleotide which specifically results in the depletion of casein kinase II catalytic subunits blocks neuritogenesis. Accordingly, this enzyme may perform an essential role during neurite growth in developing neurons. Casein kinase II depletion induced by antisense oligodeoxyribonucleotide is accompanied by a site-specific dephosphorylation of microtubule-associated protein MAP1B (also referred to as MAP5, MAP1.X or MAP1.2), which is paralleled by a release of MAP1B from microtubules. We therefore propose that phosphorylation by casein kinase II may be required for the proper MAP1B functioning in the promotion of the assembly of microtubules which constitute the cytoskeletal scaffolding of growing axon-like neurites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Casein Kinase II
  • Cell Differentiation
  • Fluorescent Antibody Technique
  • In Vitro Techniques
  • Mice
  • Microtubule-Associated Proteins / metabolism
  • Microtubules / metabolism
  • Molecular Sequence Data
  • Neurons / cytology*
  • Oligodeoxyribonucleotides / chemistry
  • Oligonucleotides, Antisense
  • Phosphorylation
  • Protein-Serine-Threonine Kinases / physiology*
  • Time Factors
  • Tumor Cells, Cultured

Substances

  • Microtubule-Associated Proteins
  • Oligodeoxyribonucleotides
  • Oligonucleotides, Antisense
  • microtubule-associated protein 1B
  • Casein Kinase II
  • Protein-Serine-Threonine Kinases