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MBC in Press, published online ahead of print December 20, 2006
Mol. Biol. Cell 10.1091/mbc.E06-08-0736

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Submitted on August 22, 2006
Revised on December 1, 2006
Accepted on December 4, 2006

Trypanosoma brucei ARF1 Plays a Central Role in Endocytosis and Golgi-Lysosome Trafficking

Helen P. Price,* Meg Stark,{dagger} and Deborah F. Smith*

*Immunology and Infection Unit and {dagger}Technology Facility, Department of Biology, University of York, Heslington, York YO10 5YW, United Kingdom

Monitoring Editor: Sean Munro

The Arf1 orthologue in the divergent eukaryote Trypanosoma brucei 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 RNAi 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 is significantly divergent from other characterized ARFs.

Address correspondence to: Deborah F. Smith (dfs501{at}york.ac.uk)




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