Plasmodium falciparum: characterization of a late asexual stage golgi protein containing both ankyrin and DHHC domains

Exp Parasitol. 2005 Aug;110(4):389-93. doi: 10.1016/j.exppara.2005.03.030.

Abstract

Proteins containing the DHHC motif have been shown to function as palmitoyl transferases. The palmitoylation of proteins has been shown to play an important role in the trafficking of proteins to the proper subcellular location. Herein, we describe a protein containing both ankyrin domains and a DHHC domain that is present in the Golgi of late schizonts of P. falciparum. The timing of expression as well as the location of this protein suggests that it may play an important role in the sorting of proteins to the apical organelles during the development of the asexual stage of the parasite.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ankyrins / chemistry*
  • Ankyrins / genetics
  • Blotting, Western
  • Carnitine O-Palmitoyltransferase / chemistry
  • Carnitine O-Palmitoyltransferase / metabolism
  • Conserved Sequence
  • Fluorescent Antibody Technique
  • Golgi Apparatus / chemistry*
  • Golgi Apparatus / enzymology
  • Immune Sera / biosynthesis
  • Immune Sera / immunology
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Plasmodium falciparum / chemistry*
  • Plasmodium falciparum / enzymology
  • Plasmodium falciparum / ultrastructure
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Ankyrins
  • Immune Sera
  • Protozoan Proteins
  • Carnitine O-Palmitoyltransferase