spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Weise, F.
Right arrow Articles by Overath, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weise, F.
Right arrow Articles by Overath, P.

Journal of Cell Science, Vol 113, Issue 24 4587-4603, Copyright © 2000 by Company of Biologists


JOURNAL ARTICLES

Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells

F Weise, YD Stierhof, C Kuhn, M Wiese and P Overath
Max-Planck-Institut fur Biologie, Abteilung Membranbiochemie, D-72076 Tubingen, Germany.

The cellular distribution of two glycosyl-phosphatidylinositol (GPI)-anchored proteins and a trans-membrane protein and the compartments involved in their trafficking were investigated in the insect stage of Leishmania mexicana, which belongs to the phylogenetically old protozoan family Trypanosomatidae. Electron microscopy of sections from high-pressure frozen and freeze-substituted cells allowed a detailed description of exo- and endocytic structures located in the vesicle-rich, densely packed anterior part of the spindle-shaped cell. A complex of tubular clusters/translucent vesicles is the prominent structure between the trans-side of the single Golgi apparatus and the flagellar pocket, the only site of endo- and exocytosis. A tubulovesicular compartment lined by one or two distinct microtubules and extending along the length of the cell is proposed to be a post-Golgi and probably late endosomal/lysosomal compartment. Using biotinylation experiments, FACS analysis and quantitative immunoelectron microscopy it was found that, at comparable expression levels, 73-75% of the two GPI-anchored proteins but only 13% of the trans-membrane protein are located on the cell surface. The tubulovesicular compartment contains 46%, the ER 5%, the Golgi complex 1.9% and the tubular cluster/translucent vesicle complex 3.6% of the intracellular fraction of the GPI-anchored protease, GP63. The density of GP63 was found to be 23-fold higher on the plasma/flagellar pocket membrane than on the ER and about tenfold higher than on membranes of the Golgi complex or of endo- or exocytic vesicles. These results indicate that there is a considerable concentration gradient of GPI-anchored proteins between the plasma/flagellar pocket membrane and the ER as well as structures involved in exo- or endocytosis. Possible mechanisms how this concentration gradient is established are discussed.


This article has been cited by other articles:


Home page
Eukaryot CellHome page
J. E. Vince, D. L. Tull, T. Spurck, M. C. Derby, G. I. McFadden, P. A. Gleeson, S. Gokool, and M. J. McConville
Leishmania Adaptor Protein-1 Subunits Are Required for Normal Lysosome Traffic, Flagellum Biogenesis, Lipid Homeostasis, and Adaptation to Temperatures Encountered in the Mammalian Host
Eukaryot. Cell, August 1, 2008; 7(8): 1256 - 1267.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
S. Besteiro, D. Tonn, L. Tetley, G. H. Coombs, and J. C. Mottram
The AP3 adaptor is involved in the transport of membrane proteins to acidocalcisomes of Leishmania
J. Cell Sci., March 1, 2008; 121(5): 561 - 570.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
C. Yao, J. E. Donelson, and M. E. Wilson
Internal and Surface-Localized Major Surface Proteases of Leishmania spp. and Their Differential Release from Promastigotes
Eukaryot. Cell, October 1, 2007; 6(10): 1905 - 1912.
[Abstract] [Full Text] [PDF]


Home page
J Med MicrobiolHome page
Ashutosh, S. Sundar, and N. Goyal
Molecular mechanisms of antimony resistance in Leishmania
J. Med. Microbiol., February 1, 2007; 56(2): 143 - 153.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Besteiro, R. A. M. Williams, L. S. Morrison, G. H. Coombs, and J. C. Mottram
Endosome Sorting and Autophagy Are Essential for Differentiation and Virulence of Leishmania major
J. Biol. Chem., April 21, 2006; 281(16): 11384 - 11396.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
Z. Zheng, R. K. Tweten, and K. Mensa-Wilmot
Intracellular Glycosylphosphatidylinositols Accumulate on Endosomes: Toxicity of Alpha-Toxin to Leishmania major
Eukaryot. Cell, March 1, 2005; 4(3): 556 - 566.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Gokool
{sigma}1- and {micro}1-Adaptin Homologues of Leishmania mexicana Are Required for Parasite Survival in the Infected Host
J. Biol. Chem., August 8, 2003; 278(32): 29400 - 29409.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
C. G. Grunfelder, M. Engstler, F. Weise, H. Schwarz, Y.-D. Stierhof, G. W. Morgan, M. C. Field, and P. Overath
Endocytosis of a Glycosylphosphatidylinositol-anchored Protein via Clathrin-coated Vesicles, Sorting by Default in Endosomes, and Exocytosis via RAB11-positive Carriers
Mol. Biol. Cell, May 1, 2003; 14(5): 2029 - 2040.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Ellis, D. K. Sharma, J. D. Hilley, G. H. Coombs, and J. C. Mottram
Processing and Trafficking of Leishmania mexicana GP63. ANALYSIS USING GPI8 MUTANTS DEFICIENT IN GLYCOSYLPHOSPHATIDYLINOSITOL PROTEIN ANCHORING
J. Biol. Chem., July 26, 2002; 277(31): 27968 - 27974.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. S. McGwire, W. A. O'Connell, K.-P. Chang, and D. M. Engman
Extracellular Release of the Glycosylphosphatidylinositol (GPI)-linked Leishmania Surface Metalloprotease, gp63, Is Independent of GPI Phospholipolysis. IMPLICATIONS FOR PARASITE VIRULENCE
J. Biol. Chem., March 8, 2002; 277(11): 8802 - 8809.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Pal, B. S. Hall, D. N. Nesbeth, H. I. Field, and M. C. Field
Differential Endocytic Functions of Trypanosoma brucei Rab5 Isoforms Reveal a Glycosylphosphatidylinositol-specific Endosomal Pathway
J. Biol. Chem., March 8, 2002; 277(11): 9529 - 9539.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
M. J. McConville, K. A. Mullin, S. C. Ilgoutz, and R. D. Teasdale
Secretory Pathway of Trypanosomatid Parasites
Microbiol. Mol. Biol. Rev., March 1, 2002; 66(1): 122 - 154.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Legare, D. Richard, R. Mukhopadhyay, Y.-D. Stierhof, B. P. Rosen, A. Haimeur, B. Papadopoulou, and M. Ouellette
The Leishmania ATP-binding Cassette Protein PGPA Is an Intracellular Metal-Thiol Transporter ATPase
J. Biol. Chem., July 6, 2001; 276(28): 26301 - 26307.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 2000