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Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway
Although actin filaments can form by oligomer annealing in vitro, they are assumed to assemble exclusively from actin monomers in vivo. In this study, we show that a pool of actin resistant to the monomer-sequestering drug latrunculin A (lat A) contributes to filament assembly in vivo. Furthermore,...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845081/ https://www.ncbi.nlm.nih.gov/pubmed/20231387 http://dx.doi.org/10.1083/jcb.200909176 |
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author | Okreglak, Voytek Drubin, David G. |
author_facet | Okreglak, Voytek Drubin, David G. |
author_sort | Okreglak, Voytek |
collection | PubMed |
description | Although actin filaments can form by oligomer annealing in vitro, they are assumed to assemble exclusively from actin monomers in vivo. In this study, we show that a pool of actin resistant to the monomer-sequestering drug latrunculin A (lat A) contributes to filament assembly in vivo. Furthermore, we show that the cofilin accessory protein Aip1 is important for establishment of normal actin monomer concentration in cells and efficiently converts cofilin-generated actin filament disassembly products into monomers and short oligomers in vitro. Additionally, in aip1Δ mutant cells, lat A–insensitive actin assembly is significantly enhanced. We conclude that actin oligomer annealing is a physiologically relevant actin filament assembly pathway in vivo and identify Aip1 as a crucial factor for shifting the distribution of short actin oligomers toward monomers during disassembly. |
format | Text |
id | pubmed-2845081 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28450812010-09-22 Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway Okreglak, Voytek Drubin, David G. J Cell Biol Research Articles Although actin filaments can form by oligomer annealing in vitro, they are assumed to assemble exclusively from actin monomers in vivo. In this study, we show that a pool of actin resistant to the monomer-sequestering drug latrunculin A (lat A) contributes to filament assembly in vivo. Furthermore, we show that the cofilin accessory protein Aip1 is important for establishment of normal actin monomer concentration in cells and efficiently converts cofilin-generated actin filament disassembly products into monomers and short oligomers in vitro. Additionally, in aip1Δ mutant cells, lat A–insensitive actin assembly is significantly enhanced. We conclude that actin oligomer annealing is a physiologically relevant actin filament assembly pathway in vivo and identify Aip1 as a crucial factor for shifting the distribution of short actin oligomers toward monomers during disassembly. The Rockefeller University Press 2010-03-22 /pmc/articles/PMC2845081/ /pubmed/20231387 http://dx.doi.org/10.1083/jcb.200909176 Text en © 2010 Okreglak and Drubin 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Okreglak, Voytek Drubin, David G. Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title | Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title_full | Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title_fullStr | Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title_full_unstemmed | Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title_short | Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
title_sort | loss of aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2845081/ https://www.ncbi.nlm.nih.gov/pubmed/20231387 http://dx.doi.org/10.1083/jcb.200909176 |
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