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Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane
Endocytosis in yeast requires actin and clathrin. Live cell imaging has previously shown that massive actin polymerization occurs concomitant with a slow 200-nm inward movement of the endocytic coat (Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. Cell. 115:475–487). However, the nature of the primary...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2290847/ https://www.ncbi.nlm.nih.gov/pubmed/18347067 http://dx.doi.org/10.1083/jcb.200708060 |
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author | Idrissi, Fatima-Zahra Grötsch, Helga Fernández-Golbano, Isabel M. Presciatto-Baschong, Cristina Riezman, Howard Geli, María-Isabel |
author_facet | Idrissi, Fatima-Zahra Grötsch, Helga Fernández-Golbano, Isabel M. Presciatto-Baschong, Cristina Riezman, Howard Geli, María-Isabel |
author_sort | Idrissi, Fatima-Zahra |
collection | PubMed |
description | Endocytosis in yeast requires actin and clathrin. Live cell imaging has previously shown that massive actin polymerization occurs concomitant with a slow 200-nm inward movement of the endocytic coat (Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. Cell. 115:475–487). However, the nature of the primary endocytic profile in yeast and how clathrin and actin cooperate to generate an endocytic vesicle is unknown. In this study, we analyze the distribution of nine different proteins involved in endocytic uptake along plasma membrane invaginations using immunoelectron microscopy. We find that the primary endocytic profiles are tubular invaginations of up to 50 nm in diameter and 180 nm in length, which accumulate the endocytic coat components at the tip. Interestingly, significant actin labeling is only observed on invaginations longer than 50 nm, suggesting that initial membrane bending occurs before initiation of the slow inward movement. We also find that in the longest profiles, actin and the myosin-I Myo5p form two distinct structures that might be implicated in vesicle fission. |
format | Text |
id | pubmed-2290847 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22908472008-09-24 Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane Idrissi, Fatima-Zahra Grötsch, Helga Fernández-Golbano, Isabel M. Presciatto-Baschong, Cristina Riezman, Howard Geli, María-Isabel J Cell Biol Research Articles Endocytosis in yeast requires actin and clathrin. Live cell imaging has previously shown that massive actin polymerization occurs concomitant with a slow 200-nm inward movement of the endocytic coat (Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. Cell. 115:475–487). However, the nature of the primary endocytic profile in yeast and how clathrin and actin cooperate to generate an endocytic vesicle is unknown. In this study, we analyze the distribution of nine different proteins involved in endocytic uptake along plasma membrane invaginations using immunoelectron microscopy. We find that the primary endocytic profiles are tubular invaginations of up to 50 nm in diameter and 180 nm in length, which accumulate the endocytic coat components at the tip. Interestingly, significant actin labeling is only observed on invaginations longer than 50 nm, suggesting that initial membrane bending occurs before initiation of the slow inward movement. We also find that in the longest profiles, actin and the myosin-I Myo5p form two distinct structures that might be implicated in vesicle fission. The Rockefeller University Press 2008-03-24 /pmc/articles/PMC2290847/ /pubmed/18347067 http://dx.doi.org/10.1083/jcb.200708060 Text en Copyright © 2008, 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 | Research Articles Idrissi, Fatima-Zahra Grötsch, Helga Fernández-Golbano, Isabel M. Presciatto-Baschong, Cristina Riezman, Howard Geli, María-Isabel Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title | Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title_full | Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title_fullStr | Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title_full_unstemmed | Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title_short | Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane |
title_sort | distinct acto/myosin-i structures associate with endocytic profiles at the plasma membrane |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2290847/ https://www.ncbi.nlm.nih.gov/pubmed/18347067 http://dx.doi.org/10.1083/jcb.200708060 |
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