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Journal of Cell Science 115, 3253-3263 (2002)
© 2002 The Company of Biologists Limited

Research Article

Developmentally regulated trafficking of the lysosomal membrane protein p67 in Trypanosoma brucei

David L. Alexander*, Kevin J. Schwartz, Andrew E. Balber{ddagger} and James D. Bangs§

The Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, WI 53706, USA
* Present address: Department of Microbiology and Immunology, Stanford University Medical School, Fairchild Building, D305, Stanford, CA 94305, USA
{ddagger} Present address: StemCo Biomedical Inc., 2810 Meridian Parkway, Suite 148, Durham, NC 27713, USA

§ Author for correspondence (e-mail: jdbangs{at}facstaff.wisc.edu )

Accepted 28 May 2002

p67 is a lysosomal type I membrane glycoprotein of Trypanosoma brucei. In procyclic stage cells p67 trafficks to the lysosome without modification, but in the bloodstream stage Golgi processing adds poly-N-acetyllactosamine to N-glycans. In both stages proteolytic fragmentation occurs in the lysosome, but turnover is approximately nine times faster in bloodstream cells. Trafficking of wildtype p67 and mutants missing the cytoplasmic (p67{Delta}CD) or cytoplasmic/transmembrane domains (p67{Delta}TM) was monitored by pulse-chase, surface biotinylation and immunofluorescence. Overexpressed wildtype p67 trafficks normally in procyclics, but some leaks to the cell surface suggesting that the targeting machinery is saturable. p67{Delta}CD and p67{Delta}TM are delivered to the cell surface and secreted, respectively. The membrane/cytoplasmic domains function correctly in procyclic cells when fused to GFP indicating that these domains are sufficient for stage-specific lysosomal targeting. In contrast, p67 wildtype and deletion reporters are overwhelmingly targeted to the lysosome and degraded in bloodstream cells. These findings suggest that either redundant developmentally regulated targeting signals/machinery are operative in this stage or that the increased endocytic activity of bloodstream cells prevents export of the deletion reporters.

Key words: Trypanosome, Lysosome, Flagellar pocket, Endocytosis, LAMP




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© The Company of Biologists Ltd 2002