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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2012
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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. |
format | Online Article Text |
id | pubmed-3419106 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
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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