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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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Detalles Bibliográficos
Autores principales: Cai, Liang, Bear, James E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
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.
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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
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