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Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum
The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5410153/ https://www.ncbi.nlm.nih.gov/pubmed/28462015 http://dx.doi.org/10.7717/peerj.3128 |
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author | Chaudhari, Rahul Dey, Vishakha Narayan, Aishwarya Sharma, Shobhona Patankar, Swati |
author_facet | Chaudhari, Rahul Dey, Vishakha Narayan, Aishwarya Sharma, Shobhona Patankar, Swati |
author_sort | Chaudhari, Rahul |
collection | PubMed |
description | The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPx(Gl)) and inhibitors of vesicular transport. As expected, the G protein-dependent vesicular fusion inhibitor AlF(4(−)) and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted to the host cell membrane. However, while both PfTPx(Gl) and ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that G protein-dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that PfTPx(Gl) is localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways: first, the vesicular trafficking pathway appears to handle not only secretory proteins, but an apicoplast membrane protein, PfTPx(Gl); second, trafficking of apicoplast luminal proteins appear to be independent of G protein-coupled vesicles. |
format | Online Article Text |
id | pubmed-5410153 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54101532017-05-01 Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum Chaudhari, Rahul Dey, Vishakha Narayan, Aishwarya Sharma, Shobhona Patankar, Swati PeerJ Cell Biology The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPx(Gl)) and inhibitors of vesicular transport. As expected, the G protein-dependent vesicular fusion inhibitor AlF(4(−)) and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted to the host cell membrane. However, while both PfTPx(Gl) and ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that G protein-dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that PfTPx(Gl) is localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways: first, the vesicular trafficking pathway appears to handle not only secretory proteins, but an apicoplast membrane protein, PfTPx(Gl); second, trafficking of apicoplast luminal proteins appear to be independent of G protein-coupled vesicles. PeerJ Inc. 2017-04-27 /pmc/articles/PMC5410153/ /pubmed/28462015 http://dx.doi.org/10.7717/peerj.3128 Text en ©2017 Chaudhari et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Cell Biology Chaudhari, Rahul Dey, Vishakha Narayan, Aishwarya Sharma, Shobhona Patankar, Swati Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title | Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title_full | Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title_fullStr | Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title_full_unstemmed | Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title_short | Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum |
title_sort | membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite plasmodium falciparum |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5410153/ https://www.ncbi.nlm.nih.gov/pubmed/28462015 http://dx.doi.org/10.7717/peerj.3128 |
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