An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.

The basic organisation of the endomembrane system is conserved in all eukaryotes and comparative genome analyses provides compelling evidence that the endomembrane system of the last common eukaryotic ancestor (LCEA) is complex with many genes required for regulated traffic being present. Although a...

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Autores principales: Katrin Kremer, Dirk Kamin, Eva Rittweger, Jonathan Wilkes, Halley Flammer, Sabine Mahler, Joanne Heng, Christopher J Tonkin, Gordon Langsley, Stefan W Hell, Vernon B Carruthers, David J P Ferguson, Markus Meissner
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spelling oai:doaj.org-article:30d1570ac4434ff882074a756a8316642021-11-18T06:05:57ZAn overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.1553-73661553-737410.1371/journal.ppat.1003213https://doaj.org/article/30d1570ac4434ff882074a756a8316642013-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23505371/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The basic organisation of the endomembrane system is conserved in all eukaryotes and comparative genome analyses provides compelling evidence that the endomembrane system of the last common eukaryotic ancestor (LCEA) is complex with many genes required for regulated traffic being present. Although apicomplexan parasites, causative agents of severe human and animal diseases, appear to have only a basic set of trafficking factors such as Rab-GTPases, they evolved unique secretory organelles (micronemes, rhoptries and dense granules) that are sequentially secreted during invasion of the host cell. In order to define the secretory pathway of apicomplexans, we performed an overexpression screen of Rabs in Toxoplasma gondii and identified Rab5A and Rab5C as important regulators of traffic to micronemes and rhoptries. Intriguingly, we found that not all microneme proteins traffic depends on functional Rab5A and Rab5C, indicating the existence of redundant microneme targeting pathways. Using two-colour super-resolution stimulated emission depletion (STED) we verified distinct localisations of independent microneme proteins and demonstrate that micronemal organelles are organised in distinct subsets or subcompartments. Our results suggest that apicomplexan parasites modify classical regulators of the endocytic system to carryout essential parasite-specific roles in the biogenesis of their unique secretory organelles.Katrin KremerDirk KaminEva RittwegerJonathan WilkesHalley FlammerSabine MahlerJoanne HengChristopher J TonkinGordon LangsleyStefan W HellVernon B CarruthersDavid J P FergusonMarkus MeissnerPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 3, p e1003213 (2013)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Katrin Kremer
Dirk Kamin
Eva Rittweger
Jonathan Wilkes
Halley Flammer
Sabine Mahler
Joanne Heng
Christopher J Tonkin
Gordon Langsley
Stefan W Hell
Vernon B Carruthers
David J P Ferguson
Markus Meissner
An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
description The basic organisation of the endomembrane system is conserved in all eukaryotes and comparative genome analyses provides compelling evidence that the endomembrane system of the last common eukaryotic ancestor (LCEA) is complex with many genes required for regulated traffic being present. Although apicomplexan parasites, causative agents of severe human and animal diseases, appear to have only a basic set of trafficking factors such as Rab-GTPases, they evolved unique secretory organelles (micronemes, rhoptries and dense granules) that are sequentially secreted during invasion of the host cell. In order to define the secretory pathway of apicomplexans, we performed an overexpression screen of Rabs in Toxoplasma gondii and identified Rab5A and Rab5C as important regulators of traffic to micronemes and rhoptries. Intriguingly, we found that not all microneme proteins traffic depends on functional Rab5A and Rab5C, indicating the existence of redundant microneme targeting pathways. Using two-colour super-resolution stimulated emission depletion (STED) we verified distinct localisations of independent microneme proteins and demonstrate that micronemal organelles are organised in distinct subsets or subcompartments. Our results suggest that apicomplexan parasites modify classical regulators of the endocytic system to carryout essential parasite-specific roles in the biogenesis of their unique secretory organelles.
format article
author Katrin Kremer
Dirk Kamin
Eva Rittweger
Jonathan Wilkes
Halley Flammer
Sabine Mahler
Joanne Heng
Christopher J Tonkin
Gordon Langsley
Stefan W Hell
Vernon B Carruthers
David J P Ferguson
Markus Meissner
author_facet Katrin Kremer
Dirk Kamin
Eva Rittweger
Jonathan Wilkes
Halley Flammer
Sabine Mahler
Joanne Heng
Christopher J Tonkin
Gordon Langsley
Stefan W Hell
Vernon B Carruthers
David J P Ferguson
Markus Meissner
author_sort Katrin Kremer
title An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
title_short An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
title_full An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
title_fullStr An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
title_full_unstemmed An overexpression screen of Toxoplasma gondii Rab-GTPases reveals distinct transport routes to the micronemes.
title_sort overexpression screen of toxoplasma gondii rab-gtpases reveals distinct transport routes to the micronemes.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/30d1570ac4434ff882074a756a831664
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