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Published online 25 February 2002. doi:10.1083/jcb.200201036
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© The Rockefeller University Press, 0021-9525/2002/3/867 $5.00
The Journal of Cell Biology, Volume 156, Number 5, March 4, 2002 867-877

Article

 Trypanin is a cytoskeletal linker protein and is required for cell motility in African trypanosomes

Nathan R. Hutchings1,2, John E. Donelson1,2 and Kent L. Hill3

1 Department of Biochemistry, University of Iowa, Iowa City, IA 52242
2 Interdepartmental Genetics Ph.D. Program, University of Iowa, Iowa City, IA 52242
3 Department of Microbiology, Immunology, and Molecular Genetics, University of California at Los Angeles, Los Angeles, CA 90095

Address correspondence to Kent L. Hill, Dept. of Microbiology, Immunology, and Molecular Genetics, University of California at Los Angeles, 10833 Le Conte Ave., Los Angeles, CA 90095. Tel.: (310) 267-0546. Fax: (310) 206-3865. E-mail: kenthill{at}mednet.ucla.edu

The cytoskeleton of eukaryotic cells is comprised of a complex network of distinct but interconnected filament systems that function in cell division, cell motility, and subcellular trafficking of proteins and organelles. A gap in our understanding of this dynamic network is the identification of proteins that connect subsets of cytoskeletal structures. We previously discovered a family of cytoskeleton-associated proteins that includes GAS11, a candidate human tumor suppressor upregulated in growth-arrested cells, and trypanin, a component of the flagellar cytoskeleton of African trypanosomes. Although these proteins are intimately associated with the cytoskeleton, their function has yet to be determined. Here we use double-stranded RNA interference to block trypanin expression in Trypanosoma brucei, and demonstrate that this protein is required for directional cell motility. Trypanin(-) mutants have an active flagellum, but are unable to coordinate flagellar beat. As a consequence, they spin and tumble uncontrollably, occasionally moving backward. Immunofluorescence experiments demonstrate that trypanin is located along the flagellum/flagellum attachment zone and electron microscopic analysis revealed that cytoskeletal connections between the flagellar apparatus and subpellicular cytoskeleton are destabilized in trypanin(-) mutants. These results indicate that trypanin functions as a cytoskeletal linker protein and offer insights into the mechanisms of flagellum-based cell motility.

Key Words: trypanin; microtubule-associated protein; cytoskeleton; cell motility; dsRNA interference


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