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Exported J domain proteins of the human malaria parasite
The heat shock protein 40 (Hsp40) family, also called J domain proteins (JDPs), regulate their Hsp70 partners by ensuring that they are engaging the right substrate at the right time and in the right location within the cell. A number of JDPs can serve as co-chaperone for a particular Hsp70, and so...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9470956/ https://www.ncbi.nlm.nih.gov/pubmed/36120546 http://dx.doi.org/10.3389/fmolb.2022.978663 |
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author | Almaazmi, Shaikha Y. Singh, Harpreet Dutta, Tanima Blatch, Gregory L. |
author_facet | Almaazmi, Shaikha Y. Singh, Harpreet Dutta, Tanima Blatch, Gregory L. |
author_sort | Almaazmi, Shaikha Y. |
collection | PubMed |
description | The heat shock protein 40 (Hsp40) family, also called J domain proteins (JDPs), regulate their Hsp70 partners by ensuring that they are engaging the right substrate at the right time and in the right location within the cell. A number of JDPs can serve as co-chaperone for a particular Hsp70, and so one generally finds many more JDPs than Hsp70s in the cell. In humans there are 13 Hsp70s and 49 JDPs. The human malaria parasite, Plasmodium falciparum, has dedicated an unusually large proportion of its genome to molecular chaperones, with a disproportionately high number of JDPs (PfJDPs) of 49 members. Interestingly, just under half of the PfJDPs are exported into the host cell during the asexual stage of the life cycle, when the malaria parasite invades mature red blood cells. Recent evidence suggests that these PfJDPs may be functionalizing both host and parasite Hsp70s within the infected red blood cell, and thereby driving the renovation of the host cell towards pathological ends. PfJDPs have been found to localize to the host cytosol, mobile structures within the host cytosol (so called “J Dots”), the host plasma membrane, and specialized structures associated with malaria pathology such as the knobs. A number of these exported PfJDPs are essential, and there is growing experimental evidence that they are important for the survival and pathogenesis of the malaria parasite. This review critiques our understanding of the important role these exported PfJDPs play at the host-parasite interface. |
format | Online Article Text |
id | pubmed-9470956 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-94709562022-09-15 Exported J domain proteins of the human malaria parasite Almaazmi, Shaikha Y. Singh, Harpreet Dutta, Tanima Blatch, Gregory L. Front Mol Biosci Molecular Biosciences The heat shock protein 40 (Hsp40) family, also called J domain proteins (JDPs), regulate their Hsp70 partners by ensuring that they are engaging the right substrate at the right time and in the right location within the cell. A number of JDPs can serve as co-chaperone for a particular Hsp70, and so one generally finds many more JDPs than Hsp70s in the cell. In humans there are 13 Hsp70s and 49 JDPs. The human malaria parasite, Plasmodium falciparum, has dedicated an unusually large proportion of its genome to molecular chaperones, with a disproportionately high number of JDPs (PfJDPs) of 49 members. Interestingly, just under half of the PfJDPs are exported into the host cell during the asexual stage of the life cycle, when the malaria parasite invades mature red blood cells. Recent evidence suggests that these PfJDPs may be functionalizing both host and parasite Hsp70s within the infected red blood cell, and thereby driving the renovation of the host cell towards pathological ends. PfJDPs have been found to localize to the host cytosol, mobile structures within the host cytosol (so called “J Dots”), the host plasma membrane, and specialized structures associated with malaria pathology such as the knobs. A number of these exported PfJDPs are essential, and there is growing experimental evidence that they are important for the survival and pathogenesis of the malaria parasite. This review critiques our understanding of the important role these exported PfJDPs play at the host-parasite interface. Frontiers Media S.A. 2022-08-31 /pmc/articles/PMC9470956/ /pubmed/36120546 http://dx.doi.org/10.3389/fmolb.2022.978663 Text en Copyright © 2022 Almaazmi, Singh, Dutta and Blatch. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Almaazmi, Shaikha Y. Singh, Harpreet Dutta, Tanima Blatch, Gregory L. Exported J domain proteins of the human malaria parasite |
title | Exported J domain proteins of the human malaria parasite |
title_full | Exported J domain proteins of the human malaria parasite |
title_fullStr | Exported J domain proteins of the human malaria parasite |
title_full_unstemmed | Exported J domain proteins of the human malaria parasite |
title_short | Exported J domain proteins of the human malaria parasite |
title_sort | exported j domain proteins of the human malaria parasite |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9470956/ https://www.ncbi.nlm.nih.gov/pubmed/36120546 http://dx.doi.org/10.3389/fmolb.2022.978663 |
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