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An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins

Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultravio...

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Detalles Bibliográficos
Autores principales: Burgess, Hannah M., Gray, Nicola K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3419106/
https://www.ncbi.nlm.nih.gov/pubmed/22896784
http://dx.doi.org/10.4161/cib.19347
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author Burgess, Hannah M.
Gray, Nicola K.
author_facet Burgess, Hannah M.
Gray, Nicola K.
author_sort Burgess, Hannah M.
collection PubMed
description Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.
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spelling pubmed-34191062012-08-15 An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins Burgess, Hannah M. Gray, Nicola K. Commun Integr Biol Short Communication Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs. Landes Bioscience 2012-05-01 /pmc/articles/PMC3419106/ /pubmed/22896784 http://dx.doi.org/10.4161/cib.19347 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 Short Communication
Burgess, Hannah M.
Gray, Nicola K.
An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title_full An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title_fullStr An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title_full_unstemmed An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title_short An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins
title_sort integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(a)-binding proteins
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3419106/
https://www.ncbi.nlm.nih.gov/pubmed/22896784
http://dx.doi.org/10.4161/cib.19347
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