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Vol. 18, Issue 3, 864-873, March 2007

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

Helen P. Price^*, Meg Stark, and Deborah F. Smith^*

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

Submitted August 22, 2006; Revised December 1, 2006; Accepted December 4, 2006
Monitoring Editor: Sean Munro

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.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

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

Abbreviations used: Arf, ADP ribosylation factor; BFA, brefeldin A; BSF, bloodstream form; ConA, concanavalin A; CD, cytochalasin D; GEF, guanine nucleotide exchange factor; RNAi, RNA interferencep; VSG, variant surface glycoprotein.

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