Gigaxonin is associated with the Golgi and dimerises via its BTB domain

Neuroreport. 2004 Apr 9;15(5):873-6. doi: 10.1097/00001756-200404090-00028.

Abstract

Mutations in the gigaxonin gene cause giant axonal neuropathy. The amino-terminus of gigaxonin contains a BTB domain but no binding partners for this domain have so far been identified. Here, we demonstrate that the gigaxonin BTB domain forms homodimers. Other BTB-bearing proteins have also been shown to dimerise via their BTB domains with the dimers then capable of interacting with other ligands. Thus, the gigaxonin BTB domain may function in a similar manner. We also demonstrate that gigaxonin is expressed in a wide variety of neuronal cell types where a significant proportion exists in cell bodies. Confocal microscope studies of gigaxonin-transfected COS-7 cells and cultured neurones revealed that a proportion of gigaxonin localises to the Golgi and endoplasmic reticulum.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western / methods
  • Cells, Cultured
  • Chlorocebus aethiops
  • Cricetinae
  • Cricetulus
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Endoplasmic Reticulum / metabolism
  • Golgi Apparatus / metabolism*
  • Humans
  • Immunohistochemistry / methods
  • Infant, Newborn
  • Mutation
  • Neurons / metabolism*
  • Rats
  • Sequence Homology, Amino Acid
  • Transfection / methods
  • Two-Hybrid System Techniques
  • Yeasts

Substances

  • Cytoskeletal Proteins
  • DNA-Binding Proteins
  • GAN protein, human