Abstract
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 language | English |
|---|---|
| Pages (from-to) | 864-873 |
| Number of pages | 10 |
| Journal | Molecular Biology of the Cell |
| Volume | 18 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1 Mar 2007 |
Keywords
- 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