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Tip20p prohibits back-fusion of COPII vesicles with the endoplasmic reticulum (2004)

F. Kamena ; A. Spang

American Association for the Advancement of Science (AAAS)

In: Science. 304(5668): 286-9. doi: 10.1126/science.1095049.

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Publication Date: 2004-04-10

Description: Directionality in intracellular trafficking is essential to ensure the correct localization of proteins along the secretory pathway. Here, we found evidence for an active mechanism that prohibited back-fusion of de novo-generated vesicles with their donor compartment. Tip20p is a peripheral membrane protein implicated in consumption of COPI vesicles at the endoplasmic reticulum. However, a specific mutant of TIP20 did not interfere with COPII vesicle generation but allowed these vesicles to fuse back to the endoplasmic reticulum, a process that does not occur normally in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamena, Faustin -- Spang, Anne -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Laboratorium der Max Planck Gesellschaft, Spemannstrasse 39, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073376" target="_blank"〉PubMed〈/a〉

Keywords: COP-Coated Vesicles/*physiology/ultrastructure ; Carrier Proteins/genetics/*physiology ; Endoplasmic Reticulum/metabolism/*physiology/ultrastructure ; Glycoproteins/genetics/*physiology ; Golgi Apparatus/metabolism ; Intracellular Membranes/physiology/ultrastructure ; *Membrane Fusion ; Mutation ; Peptides/metabolism ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/*physiology/ultrastructure ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Vesicular Transport Proteins ; alpha-Glucosidases/genetics/metabolism

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Toxoplasma gondii secretory proteins bind to sulfated heparin structures (2012)

Azzouz, N., Kamena, F., Laurino, P., Kikkeri, R., Mercier, C., Cesbron-Delauw, M.-F., Dubremetz, J.-F., De Cola, L., Seeberger, P. H.

Oxford University Press

In: Glycobiology

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Publication Date: 2012-11-24

Description: Toxoplasma gondii is the causative agent of toxoplasmosis, one of the most widespread infections in humans and animals, and is a major opportunistic pathogen in immunocompromised patients. Toxoplasma gondii is unique as it can invade virtually any nucleated cell, although the mechanisms are not completely understood. Parasite attachment to the host cell is a prerequisite for reorientation and penetration and likely requires the recognition of molecules at the host cell surface. It has been reported that the affinity of tachyzoites, the invasive form of T. gondii , for host cells can be inhibited by a variety of soluble-sulfated glycosaminoglycans (GAGs), such as heparan sulfate. Using heparin-functionalized zeolites in the absence of host cells, we visualized heparin-binding sites on the surface of tachyzoites by confocal and atomic force microscopy. Furthermore, we report that protein components of the parasite rhoptry, dense granule and surface bind GAGs. In particular, the proteins ROP2 and ROP4 from the rhoptry, GRA2 from the dense granules and the surface protein SAG1 were found to bind heparin. The binding specificities and affinities of individual parasite proteins for natural heparin and heparin oligosaccharides were determined by a combination of heparin oligosaccharide microarrays and surface plasmon resonance. Our results suggest that interactions between sulfated GAGs and parasite surface antigens contribute to T. gondii attachment to host cell surfaces as well as initiating the invasion process, while rhoptries and dense granule organelles may play an important role during the establishment of the infection and during the life of the parasite inside the parasitophorous vacuole.

Print ISSN: 0959-6658

Electronic ISSN: 1460-2423

Topics: Biology , Medicine