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Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus
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Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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Personen und Körperschaften: | , |
In: | Proceedings of the National Academy of Sciences, 105, 2008, 33, S. 11790-11795 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Proceedings of the National Academy of Sciences
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Schlagwörter: |
author_facet |
Chen, Chen Zhuang, Xiaowei Chen, Chen Zhuang, Xiaowei |
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author |
Chen, Chen Zhuang, Xiaowei |
spellingShingle |
Chen, Chen Zhuang, Xiaowei Proceedings of the National Academy of Sciences Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus Multidisciplinary |
author_sort |
chen, chen |
spelling |
Chen, Chen Zhuang, Xiaowei 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0803711105 <jats:p>During clathrin-mediated endocytosis, adaptor proteins recognize specific internalization signals on cargo receptors, either recruiting cargos into clathrin-coated pits (CCPs) or initiating clathrin-coat assembly around the cargo molecules. Here, we identify epsin 1, a clathrin-, ubiquitin-, and phospholipid-interacting protein, as a cargo-specific adaptor for influenza virus entry through the clathrin-mediated pathway. Using live-cell imaging to monitor the entry of individual virus particles, we observed recruitment of epsin 1 to the binding sites of influenza viruses in synchrony with the assembly of CCPs. Epsin 1 knockdown by siRNA significantly inhibited the clathrin-mediated endocytosis of the influenza virus and caused the majority of the virus particles to enter through a clathrin-independent pathway. The same treatment did not affect the entry of several classical ligands for clathrin-mediated endocytosis, including transferrin, LDL, and EGF. Overexpression of the dominant-negative epsin 1 mutant lacking the ubiquitin-interaction motifs nearly completely blocked the clathrin-mediated entry of the influenza virus without affecting transferrin uptake. These results suggest that epsin 1 functions as a cargo-specific adaptor for the clathrin-mediated entry of the influenza virus.</jats:p> Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus Proceedings of the National Academy of Sciences |
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10.1073/pnas.0803711105 |
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Proceedings of the National Academy of Sciences, 2008 |
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Proceedings of the National Academy of Sciences, 2008 |
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2008 |
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Proceedings of the National Academy of Sciences |
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title |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_unstemmed |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_full |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_fullStr |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_full_unstemmed |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_short |
Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_sort |
epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
topic |
Multidisciplinary |
url |
http://dx.doi.org/10.1073/pnas.0803711105 |
publishDate |
2008 |
physical |
11790-11795 |
description |
<jats:p>During clathrin-mediated endocytosis, adaptor proteins recognize specific internalization signals on cargo receptors, either recruiting cargos into clathrin-coated pits (CCPs) or initiating clathrin-coat assembly around the cargo molecules. Here, we identify epsin 1, a clathrin-, ubiquitin-, and phospholipid-interacting protein, as a cargo-specific adaptor for influenza virus entry through the clathrin-mediated pathway. Using live-cell imaging to monitor the entry of individual virus particles, we observed recruitment of epsin 1 to the binding sites of influenza viruses in synchrony with the assembly of CCPs. Epsin 1 knockdown by siRNA significantly inhibited the clathrin-mediated endocytosis of the influenza virus and caused the majority of the virus particles to enter through a clathrin-independent pathway. The same treatment did not affect the entry of several classical ligands for clathrin-mediated endocytosis, including transferrin, LDL, and EGF. Overexpression of the dominant-negative epsin 1 mutant lacking the ubiquitin-interaction motifs nearly completely blocked the clathrin-mediated entry of the influenza virus without affecting transferrin uptake. These results suggest that epsin 1 functions as a cargo-specific adaptor for the clathrin-mediated entry of the influenza virus.</jats:p> |
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author | Chen, Chen, Zhuang, Xiaowei |
author_facet | Chen, Chen, Zhuang, Xiaowei, Chen, Chen, Zhuang, Xiaowei |
author_sort | chen, chen |
container_issue | 33 |
container_start_page | 11790 |
container_title | Proceedings of the National Academy of Sciences |
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description | <jats:p>During clathrin-mediated endocytosis, adaptor proteins recognize specific internalization signals on cargo receptors, either recruiting cargos into clathrin-coated pits (CCPs) or initiating clathrin-coat assembly around the cargo molecules. Here, we identify epsin 1, a clathrin-, ubiquitin-, and phospholipid-interacting protein, as a cargo-specific adaptor for influenza virus entry through the clathrin-mediated pathway. Using live-cell imaging to monitor the entry of individual virus particles, we observed recruitment of epsin 1 to the binding sites of influenza viruses in synchrony with the assembly of CCPs. Epsin 1 knockdown by siRNA significantly inhibited the clathrin-mediated endocytosis of the influenza virus and caused the majority of the virus particles to enter through a clathrin-independent pathway. The same treatment did not affect the entry of several classical ligands for clathrin-mediated endocytosis, including transferrin, LDL, and EGF. Overexpression of the dominant-negative epsin 1 mutant lacking the ubiquitin-interaction motifs nearly completely blocked the clathrin-mediated entry of the influenza virus without affecting transferrin uptake. These results suggest that epsin 1 functions as a cargo-specific adaptor for the clathrin-mediated entry of the influenza virus.</jats:p> |
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spelling | Chen, Chen Zhuang, Xiaowei 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0803711105 <jats:p>During clathrin-mediated endocytosis, adaptor proteins recognize specific internalization signals on cargo receptors, either recruiting cargos into clathrin-coated pits (CCPs) or initiating clathrin-coat assembly around the cargo molecules. Here, we identify epsin 1, a clathrin-, ubiquitin-, and phospholipid-interacting protein, as a cargo-specific adaptor for influenza virus entry through the clathrin-mediated pathway. Using live-cell imaging to monitor the entry of individual virus particles, we observed recruitment of epsin 1 to the binding sites of influenza viruses in synchrony with the assembly of CCPs. Epsin 1 knockdown by siRNA significantly inhibited the clathrin-mediated endocytosis of the influenza virus and caused the majority of the virus particles to enter through a clathrin-independent pathway. The same treatment did not affect the entry of several classical ligands for clathrin-mediated endocytosis, including transferrin, LDL, and EGF. Overexpression of the dominant-negative epsin 1 mutant lacking the ubiquitin-interaction motifs nearly completely blocked the clathrin-mediated entry of the influenza virus without affecting transferrin uptake. These results suggest that epsin 1 functions as a cargo-specific adaptor for the clathrin-mediated entry of the influenza virus.</jats:p> Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus Proceedings of the National Academy of Sciences |
spellingShingle | Chen, Chen, Zhuang, Xiaowei, Proceedings of the National Academy of Sciences, Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus, Multidisciplinary |
title | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_full | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_fullStr | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_full_unstemmed | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_short | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_sort | epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
title_unstemmed | Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus |
topic | Multidisciplinary |
url | http://dx.doi.org/10.1073/pnas.0803711105 |