Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome

Histochem Cell Biol. 2006 Aug;126(2):251-9. doi: 10.1007/s00418-006-0166-5. Epub 2006 Mar 14.

Abstract

In vertebrate cells, the centrosome consists of a pair of centrioles and surrounding pericentriolar material. Using anti-Golgi 58K protein antibodies that recognize formiminotransferase cyclodeaminase (FTCD), we investigated its localization to the centrosome in various cultured cells and human oviductal secretory cells by immunohistochemistry. In addition to the Golgi apparatus, FTCD was localized to the centrosome, more abundantly around the mother centriole. The centrosome localization of FTCD continued throughout the cell cycle and was not disrupted after Golgi fragmentation, which was induced by colcemid and brefeldin A. Centriole microtubules are polyglutamylated and stable against tubulin depolymerizing drugs. FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonia-Lyases / metabolism*
  • Animals
  • Brefeldin A / pharmacology
  • Cell Cycle
  • Cells, Cultured
  • Centrioles / drug effects
  • Centrioles / physiology
  • Centrioles / ultrastructure
  • Centrosome / drug effects
  • Centrosome / metabolism*
  • Centrosome / ultrastructure
  • Chlorocebus aethiops
  • Demecolcine / pharmacology
  • Golgi Apparatus / drug effects
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Humans
  • Mice
  • Microscopy, Fluorescence
  • Microscopy, Immunoelectron
  • Microtubules / drug effects
  • Microtubules / metabolism
  • Microtubules / ultrastructure
  • Polyglutamic Acid / metabolism
  • Tubulin Modulators / pharmacology

Substances

  • Tubulin Modulators
  • Brefeldin A
  • Polyglutamic Acid
  • Ammonia-Lyases
  • formiminotetrahydrofolate cyclodeaminase
  • Demecolcine