Trypanosoma brucei ARF1 plays a central role in endocytosis and Golgi-lysosome trafficking

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The ADP ribosylation factor (Arf)1 orthologue in the divergent eukaryote Trypanosoma brucei (Tb) shares characteristics with both Arf1 and Arf6 and has a vital role in intracellular protein trafficking. TbARF1 is Golgi localized in trypanosomes but associates with the plasma membrane when expressed in human cells. Depletion of TbARF1 by RNA interference causes a major decrease in endocytosis, which correlates with Rab5 dissociation from early endosomes. Although the Golgi remains intact, parasites display enlarged flagellar pockets and intracellular flagella. An increase in active GTP-bound TbARF1 in bloodstream parasites is rapidly lethal, correlating with a defect in Golgi-to-lysosome transport. We conclude that the essential Golgi-localizing T. brucei ARF1 has a primary role in the maintenance of both post-Golgi transport and endocytosis and that it is significantly divergent from other characterized ARFs.

Original languageEnglish
Pages (from-to)864-873
Number of pages10
JournalMolecular Biology of the Cell
Issue number3
Publication statusPublished - 1 Mar 2007


  • ADP-Ribosylation Factor 1
  • ADP-Ribosylation Factors
  • Amino Acid Sequence
  • Animals
  • Cell Membrane
  • Cell Survival
  • Down-Regulation
  • Endocytosis
  • Exocytosis
  • Gene Expression
  • Golgi Apparatus
  • Guanosine Triphosphate
  • Humans
  • Lysosomes
  • Microbodies
  • Mutant Proteins
  • Protein Transport
  • RNA Interference
  • Trypanosoma brucei brucei
  • Variant Surface Glycoproteins, Trypanosoma

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