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Protein Kinase Cepsilon Actin-binding Site Is Important for Neurite Outgrowth during Neuronal Differentiation.

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Author

Summary, in English

We have previously shown that protein kinase Cepsilon (PKCepsilon) induces neurite outgrowth via its regulatory domain and independently of its kinase activity. This study aimed at identifying mechanisms regulating PKCepsilon-mediated neurite induction. We show an increased association of PKCepsilon to the cytoskeleton during neuronal differentiation. Furthermore, neurite induction by overexpression of full-length PKCepsilon is suppressed if serum is removed from the cultures or if an actin-binding site is deleted from the protein. A peptide corresponding to the PKCepsilon actin-binding site suppresses neurite outgrowth during neuronal differentiation and outgrowth elicited by PKCepsilon overexpression. Neither serum removal, deletion of the actin-binding site, nor introduction of the peptide affects neurite induction by the isolated regulatory domain. Membrane targeting by myristoylation renders full-length PKCepsilon independent of both serum and the actin-binding site, and PKCepsilon colocalized with F-actin at the cortical cytoskeleton during neurite outgrowth. These results demonstrate that the actin-binding site is of importance for signals acting on PKCepsilon in a pathway leading to neurite outgrowth. Localization of PKCepsilon to the plasma membrane and/or the cortical cytoskeleton is conceivably important for its effect on neurite outgrowth.

Publishing year

2002

Language

English

Pages

12-24

Publication/Series

Molecular Biology of the Cell

Volume

13

Issue

1

Document type

Journal article

Publisher

American Society for Cell Biology

Topic

  • Cancer and Oncology

Keywords

  • Image Cytometry
  • Microscopy
  • Confocal
  • Fluorescence
  • Neurites/*physiology
  • Neuroblastoma
  • Protein Conformation
  • Protein Kinase C/*chemistry/genetics/*metabolism
  • Recombinant Fusion Proteins/metabolism
  • Substrate Specificity
  • Support
  • Non-U.S. Gov't
  • Transfection
  • Cultured
  • Tumor Cells
  • Isoenzymes/*chemistry/genetics/*metabolism
  • Human
  • Cytoskeleton/metabolism
  • Cell Differentiation/physiology
  • Binding Sites
  • Actins/*metabolism

Status

Published

ISBN/ISSN/Other

  • ISSN: 1939-4586