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Peering deeply inside the branch
The actin-related protein 2/3 (Arp2/3) story has captivated the cytoskeleton community for over a decade. Not only does this complex nucleate new actin filaments, but it also anchors them into a dendritic meshwork that is used in many cellular contexts such as lamellipodial protrusion, endosome rock...
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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/PMC2265395/ https://www.ncbi.nlm.nih.gov/pubmed/18316414 http://dx.doi.org/10.1083/jcb.200802062 |
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author | Cai, Liang Bear, James E. |
author_facet | Cai, Liang Bear, James E. |
author_sort | Cai, Liang |
collection | PubMed |
description | The actin-related protein 2/3 (Arp2/3) story has captivated the cytoskeleton community for over a decade. Not only does this complex nucleate new actin filaments, but it also anchors them into a dendritic meshwork that is used in many cellular contexts such as lamellipodial protrusion, endosome rocketing, and the movement of pathogens. One key piece of this puzzle that has been missing is a detailed structure of the Arp2/3-actin branch. Using electron tomography and computational docking, Rouiller et al. (Rouiller, I., X.-P. Xu, K.J. Amann, C. Egile, S. Nickell, D. Nicastro, R. Li, T.D. Pollard, N. Volkmann, and D. Hanein. 2008. J. Cell Biol. 180:887–895) present an elegant and intriguing structure of the Arp2/3 complex–mediated actin branch. |
format | Text |
id | pubmed-2265395 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22653952008-09-10 Peering deeply inside the branch Cai, Liang Bear, James E. J Cell Biol Reviews The actin-related protein 2/3 (Arp2/3) story has captivated the cytoskeleton community for over a decade. Not only does this complex nucleate new actin filaments, but it also anchors them into a dendritic meshwork that is used in many cellular contexts such as lamellipodial protrusion, endosome rocketing, and the movement of pathogens. One key piece of this puzzle that has been missing is a detailed structure of the Arp2/3-actin branch. Using electron tomography and computational docking, Rouiller et al. (Rouiller, I., X.-P. Xu, K.J. Amann, C. Egile, S. Nickell, D. Nicastro, R. Li, T.D. Pollard, N. Volkmann, and D. Hanein. 2008. J. Cell Biol. 180:887–895) present an elegant and intriguing structure of the Arp2/3 complex–mediated actin branch. The Rockefeller University Press 2008-03-10 /pmc/articles/PMC2265395/ /pubmed/18316414 http://dx.doi.org/10.1083/jcb.200802062 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 | Reviews Cai, Liang Bear, James E. Peering deeply inside the branch |
title | Peering deeply inside the branch |
title_full | Peering deeply inside the branch |
title_fullStr | Peering deeply inside the branch |
title_full_unstemmed | Peering deeply inside the branch |
title_short | Peering deeply inside the branch |
title_sort | peering deeply inside the branch |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265395/ https://www.ncbi.nlm.nih.gov/pubmed/18316414 http://dx.doi.org/10.1083/jcb.200802062 |
work_keys_str_mv | AT cailiang peeringdeeplyinsidethebranch AT bearjamese peeringdeeplyinsidethebranch |