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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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Detalles Bibliográficos
Autores principales: Okreglak, Voytek, Drubin, David G.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
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.
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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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