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The Phagosome Proteome: Insight into Phagosome Functions
Phagosomes are key organelles for the innate ability of macrophages to participate in tissue remodeling, clear apoptotic cells, and restrict the spread of intracellular pathogens. To understand the functions of phagosomes, we initiated the systematic identification of their proteins. Using a proteom...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2001
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193653/ https://www.ncbi.nlm.nih.gov/pubmed/11149929 |
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author | Garin, Jérome Diez, Roberto Kieffer, Sylvie Dermine, Jean-François Duclos, Sophie Gagnon, Etienne Sadoul, Remy Rondeau, Christiane Desjardins, Michel |
author_facet | Garin, Jérome Diez, Roberto Kieffer, Sylvie Dermine, Jean-François Duclos, Sophie Gagnon, Etienne Sadoul, Remy Rondeau, Christiane Desjardins, Michel |
author_sort | Garin, Jérome |
collection | PubMed |
description | Phagosomes are key organelles for the innate ability of macrophages to participate in tissue remodeling, clear apoptotic cells, and restrict the spread of intracellular pathogens. To understand the functions of phagosomes, we initiated the systematic identification of their proteins. Using a proteomic approach, we identified >140 proteins associated with latex bead–containing phagosomes. Among these were hydrolases, proton pump ATPase subunits, and proteins of the fusion machinery, validating our approach. A series of unexpected proteins not previously described along the endocytic/phagocytic pathways were also identified, including the apoptotic proteins galectin3, Alix, and TRAIL, the anti-apoptotic protein 14-3-3, the lipid raft-enriched flotillin-1, the anti-microbial molecule lactadherin, and the small GTPase rab14. In addition, 24 spots from which the peptide masses could not be matched to entries in any database potentially represent new phagosomal proteins. The elaboration of a two-dimensional gel database of >160 identified spots allowed us to analyze how phagosome composition is modulated during phagolysosome biogenesis. Remarkably, during this process, hydrolases are not delivered in bulk to phagosomes, but are instead acquired sequentially. The systematic characterization of phagosome proteins provided new insights into phagosome functions and the protein or groups of proteins involved in and regulating these functions. |
format | Text |
id | pubmed-2193653 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2001 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21936532008-05-01 The Phagosome Proteome: Insight into Phagosome Functions Garin, Jérome Diez, Roberto Kieffer, Sylvie Dermine, Jean-François Duclos, Sophie Gagnon, Etienne Sadoul, Remy Rondeau, Christiane Desjardins, Michel J Cell Biol Original Article Phagosomes are key organelles for the innate ability of macrophages to participate in tissue remodeling, clear apoptotic cells, and restrict the spread of intracellular pathogens. To understand the functions of phagosomes, we initiated the systematic identification of their proteins. Using a proteomic approach, we identified >140 proteins associated with latex bead–containing phagosomes. Among these were hydrolases, proton pump ATPase subunits, and proteins of the fusion machinery, validating our approach. A series of unexpected proteins not previously described along the endocytic/phagocytic pathways were also identified, including the apoptotic proteins galectin3, Alix, and TRAIL, the anti-apoptotic protein 14-3-3, the lipid raft-enriched flotillin-1, the anti-microbial molecule lactadherin, and the small GTPase rab14. In addition, 24 spots from which the peptide masses could not be matched to entries in any database potentially represent new phagosomal proteins. The elaboration of a two-dimensional gel database of >160 identified spots allowed us to analyze how phagosome composition is modulated during phagolysosome biogenesis. Remarkably, during this process, hydrolases are not delivered in bulk to phagosomes, but are instead acquired sequentially. The systematic characterization of phagosome proteins provided new insights into phagosome functions and the protein or groups of proteins involved in and regulating these functions. The Rockefeller University Press 2001-01-08 /pmc/articles/PMC2193653/ /pubmed/11149929 Text en © 2001 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Original Article Garin, Jérome Diez, Roberto Kieffer, Sylvie Dermine, Jean-François Duclos, Sophie Gagnon, Etienne Sadoul, Remy Rondeau, Christiane Desjardins, Michel The Phagosome Proteome: Insight into Phagosome Functions |
title | The Phagosome Proteome: Insight into Phagosome Functions |
title_full | The Phagosome Proteome: Insight into Phagosome Functions |
title_fullStr | The Phagosome Proteome: Insight into Phagosome Functions |
title_full_unstemmed | The Phagosome Proteome: Insight into Phagosome Functions |
title_short | The Phagosome Proteome: Insight into Phagosome Functions |
title_sort | phagosome proteome: insight into phagosome functions |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193653/ https://www.ncbi.nlm.nih.gov/pubmed/11149929 |
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