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A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin
Many RNA-binding proteins (RBPs) dynamically shuttle between the nucleus and the cytoplasm, often exerting different functions in each compartment. Therefore, the nucleo-cytoplasmic distribution of RBPs has a strong impact on their activity. Here we describe the localization and the shuttling proper...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3739726/ https://www.ncbi.nlm.nih.gov/pubmed/23951221 http://dx.doi.org/10.1371/journal.pone.0071686 |
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author | Twyffels, Laure Wauquier, Corinne Soin, Romuald Decaestecker, Christine Gueydan, Cyril Kruys, Véronique |
author_facet | Twyffels, Laure Wauquier, Corinne Soin, Romuald Decaestecker, Christine Gueydan, Cyril Kruys, Véronique |
author_sort | Twyffels, Laure |
collection | PubMed |
description | Many RNA-binding proteins (RBPs) dynamically shuttle between the nucleus and the cytoplasm, often exerting different functions in each compartment. Therefore, the nucleo-cytoplasmic distribution of RBPs has a strong impact on their activity. Here we describe the localization and the shuttling properties of the tandem zinc finger RBP dTIS11, which is the Drosophila homolog of mammalian TIS11 proteins. Drosophila and mammalian TIS11 proteins act as destabilizing factors in ARE-mediated decay. At equilibrium, dTIS11 is concentrated mainly in the cytoplasm. We show that dTIS11 is a nucleo-cytoplasmic shuttling protein whose nuclear export is mediated by the exportin CRM1 through the recognition of a nuclear export signal (NES) located in a different region comparatively to its mammalian homologs. We also identify a cryptic Transportin-dependent PY nuclear localization signal (PY-NLS) in the tandem zinc finger region of dTIS11 and show that it is conserved across the TIS11 protein family. This NLS partially overlaps the second zinc finger ZnF2. Importantly, mutations disrupting the capacity of the ZnF2 to coordinate a Zinc ion unmask dTIS11 and TTP NLS and promote nuclear import. All together, our results indicate that the nuclear export of TIS11 proteins is mediated by CRM1 through diverging NESs, while their nuclear import mechanism may rely on a highly conserved PY-NLS whose activity is negatively regulated by ZnF2 folding. |
format | Online Article Text |
id | pubmed-3739726 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37397262013-08-15 A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin Twyffels, Laure Wauquier, Corinne Soin, Romuald Decaestecker, Christine Gueydan, Cyril Kruys, Véronique PLoS One Research Article Many RNA-binding proteins (RBPs) dynamically shuttle between the nucleus and the cytoplasm, often exerting different functions in each compartment. Therefore, the nucleo-cytoplasmic distribution of RBPs has a strong impact on their activity. Here we describe the localization and the shuttling properties of the tandem zinc finger RBP dTIS11, which is the Drosophila homolog of mammalian TIS11 proteins. Drosophila and mammalian TIS11 proteins act as destabilizing factors in ARE-mediated decay. At equilibrium, dTIS11 is concentrated mainly in the cytoplasm. We show that dTIS11 is a nucleo-cytoplasmic shuttling protein whose nuclear export is mediated by the exportin CRM1 through the recognition of a nuclear export signal (NES) located in a different region comparatively to its mammalian homologs. We also identify a cryptic Transportin-dependent PY nuclear localization signal (PY-NLS) in the tandem zinc finger region of dTIS11 and show that it is conserved across the TIS11 protein family. This NLS partially overlaps the second zinc finger ZnF2. Importantly, mutations disrupting the capacity of the ZnF2 to coordinate a Zinc ion unmask dTIS11 and TTP NLS and promote nuclear import. All together, our results indicate that the nuclear export of TIS11 proteins is mediated by CRM1 through diverging NESs, while their nuclear import mechanism may rely on a highly conserved PY-NLS whose activity is negatively regulated by ZnF2 folding. Public Library of Science 2013-08-09 /pmc/articles/PMC3739726/ /pubmed/23951221 http://dx.doi.org/10.1371/journal.pone.0071686 Text en © 2013 Twyffels et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Twyffels, Laure Wauquier, Corinne Soin, Romuald Decaestecker, Christine Gueydan, Cyril Kruys, Véronique A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title | A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title_full | A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title_fullStr | A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title_full_unstemmed | A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title_short | A Masked PY-NLS in Drosophila TIS11 and Its Mammalian Homolog Tristetraprolin |
title_sort | masked py-nls in drosophila tis11 and its mammalian homolog tristetraprolin |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3739726/ https://www.ncbi.nlm.nih.gov/pubmed/23951221 http://dx.doi.org/10.1371/journal.pone.0071686 |
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