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Co-transcriptional nuclear actin dynamics

Actin is a key player for nuclear structure and function regulating both chromosome organization and gene activity. In the cell nucleus actin interacts with many different proteins. Among these proteins several studies have identified classical nuclear factors involved in chromatin structure and fun...

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Autor principal: Percipalle, Piergiorgio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585027/
https://www.ncbi.nlm.nih.gov/pubmed/23138849
http://dx.doi.org/10.4161/nucl.22798
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author Percipalle, Piergiorgio
author_facet Percipalle, Piergiorgio
author_sort Percipalle, Piergiorgio
collection PubMed
description Actin is a key player for nuclear structure and function regulating both chromosome organization and gene activity. In the cell nucleus actin interacts with many different proteins. Among these proteins several studies have identified classical nuclear factors involved in chromatin structure and function, transcription and RNA processing as well as proteins that are normally involved in controlling the actin cytoskeleton. These discoveries have raised the possibility that nuclear actin performs its multi task activities through tight interactions with different sets of proteins. This high degree of promiscuity in the spectrum of protein-to-protein interactions correlates well with the conformational plasticity of actin and the ability to undergo regulated changes in its polymerization states. Several of the factors involved in controlling head-to-tail actin polymerization have been shown to be in the nucleus where they seem to regulate gene activity. By focusing on the multiple tasks performed by actin and actin-binding proteins, possible models of how actin dynamics controls the different phases of the RNA polymerase II transcription cycle are being identified.
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spelling pubmed-35850272013-03-11 Co-transcriptional nuclear actin dynamics Percipalle, Piergiorgio Nucleus Review Actin is a key player for nuclear structure and function regulating both chromosome organization and gene activity. In the cell nucleus actin interacts with many different proteins. Among these proteins several studies have identified classical nuclear factors involved in chromatin structure and function, transcription and RNA processing as well as proteins that are normally involved in controlling the actin cytoskeleton. These discoveries have raised the possibility that nuclear actin performs its multi task activities through tight interactions with different sets of proteins. This high degree of promiscuity in the spectrum of protein-to-protein interactions correlates well with the conformational plasticity of actin and the ability to undergo regulated changes in its polymerization states. Several of the factors involved in controlling head-to-tail actin polymerization have been shown to be in the nucleus where they seem to regulate gene activity. By focusing on the multiple tasks performed by actin and actin-binding proteins, possible models of how actin dynamics controls the different phases of the RNA polymerase II transcription cycle are being identified. Landes Bioscience 2013-01-01 /pmc/articles/PMC3585027/ /pubmed/23138849 http://dx.doi.org/10.4161/nucl.22798 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Percipalle, Piergiorgio
Co-transcriptional nuclear actin dynamics
title Co-transcriptional nuclear actin dynamics
title_full Co-transcriptional nuclear actin dynamics
title_fullStr Co-transcriptional nuclear actin dynamics
title_full_unstemmed Co-transcriptional nuclear actin dynamics
title_short Co-transcriptional nuclear actin dynamics
title_sort co-transcriptional nuclear actin dynamics
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3585027/
https://www.ncbi.nlm.nih.gov/pubmed/23138849
http://dx.doi.org/10.4161/nucl.22798
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