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Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis
Actin cytoskeleton remodeling is fundamental for Fcγ receptor–driven phagocytosis. In this study, we find that the leukocyte-specific protein 1 (LSP1) localizes to nascent phagocytic cups during Fcγ receptor–mediated phagocytosis, where it displays the same spatial and temporal distribution as the a...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436777/ https://www.ncbi.nlm.nih.gov/pubmed/25717183 http://dx.doi.org/10.1091/mbc.E14-05-1005 |
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author | Maxeiner, Sebastian Shi, Nian Schalla, Carmen Aydin, Guelcan Hoss, Mareike Vogel, Simon Zenke, Martin Sechi, Antonio S. |
author_facet | Maxeiner, Sebastian Shi, Nian Schalla, Carmen Aydin, Guelcan Hoss, Mareike Vogel, Simon Zenke, Martin Sechi, Antonio S. |
author_sort | Maxeiner, Sebastian |
collection | PubMed |
description | Actin cytoskeleton remodeling is fundamental for Fcγ receptor–driven phagocytosis. In this study, we find that the leukocyte-specific protein 1 (LSP1) localizes to nascent phagocytic cups during Fcγ receptor–mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcγ receptor–mediated phagocytosis. We also find that LSP1 binds to the class I molecular motor myosin1e. LSP1 interacts with the SH3 domain of myosin1e, and the localization and dynamics of both proteins in nascent phagocytic cups mirror those of actin. Furthermore, inhibition of LSP1–myosin1e and LSP1–actin interactions profoundly impairs pseudopodial formation around opsonized targets and their subsequent internalization. Thus the LSP1–myosin1e bimolecular complex plays a pivotal role in the regulation of actin cytoskeleton remodeling during Fcγ receptor–driven phagocytosis. |
format | Online Article Text |
id | pubmed-4436777 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-44367772015-07-16 Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis Maxeiner, Sebastian Shi, Nian Schalla, Carmen Aydin, Guelcan Hoss, Mareike Vogel, Simon Zenke, Martin Sechi, Antonio S. Mol Biol Cell Articles Actin cytoskeleton remodeling is fundamental for Fcγ receptor–driven phagocytosis. In this study, we find that the leukocyte-specific protein 1 (LSP1) localizes to nascent phagocytic cups during Fcγ receptor–mediated phagocytosis, where it displays the same spatial and temporal distribution as the actin cytoskeleton. Down-regulation of LSP1 severely reduces the phagocytic activity of macrophages, clearly demonstrating a crucial role for this protein in Fcγ receptor–mediated phagocytosis. We also find that LSP1 binds to the class I molecular motor myosin1e. LSP1 interacts with the SH3 domain of myosin1e, and the localization and dynamics of both proteins in nascent phagocytic cups mirror those of actin. Furthermore, inhibition of LSP1–myosin1e and LSP1–actin interactions profoundly impairs pseudopodial formation around opsonized targets and their subsequent internalization. Thus the LSP1–myosin1e bimolecular complex plays a pivotal role in the regulation of actin cytoskeleton remodeling during Fcγ receptor–driven phagocytosis. The American Society for Cell Biology 2015-05-01 /pmc/articles/PMC4436777/ /pubmed/25717183 http://dx.doi.org/10.1091/mbc.E14-05-1005 Text en © 2015 Maxeiner et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Maxeiner, Sebastian Shi, Nian Schalla, Carmen Aydin, Guelcan Hoss, Mareike Vogel, Simon Zenke, Martin Sechi, Antonio S. Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title | Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title_full | Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title_fullStr | Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title_full_unstemmed | Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title_short | Crucial role for the LSP1–myosin1e bimolecular complex in the regulation of Fcγ receptor–driven phagocytosis |
title_sort | crucial role for the lsp1–myosin1e bimolecular complex in the regulation of fcγ receptor–driven phagocytosis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436777/ https://www.ncbi.nlm.nih.gov/pubmed/25717183 http://dx.doi.org/10.1091/mbc.E14-05-1005 |
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