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Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3
14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171942/ https://www.ncbi.nlm.nih.gov/pubmed/15883195 http://dx.doi.org/10.1083/jcb.200411169 |
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author | Faul, Christian Hüttelmaier, Stefan Oh, Jun Hachet, Virginie Singer, Robert H. Mundel, Peter |
author_facet | Faul, Christian Hüttelmaier, Stefan Oh, Jun Hachet, Virginie Singer, Robert H. Mundel, Peter |
author_sort | Faul, Christian |
collection | PubMed |
description | 14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3-3 in mediating nuclear import has been described. There is also mounting evidence that nuclear import is regulated by the phosphorylation of cargo proteins, but the underlying mechanism remains elusive. Myopodin is a dual-compartment, actin-bundling protein that functions as a tumor suppressor in human bladder cancer. In muscle cells, myopodin redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. We show that importin α binding and the subsequent nuclear import of myopodin are regulated by the serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3. These results establish a novel paradigm for the promotion of nuclear import by 14-3-3 binding. They provide a molecular explanation for the phosphorylation-dependent nuclear import of nuclear localization signal-containing cargo proteins. |
format | Text |
id | pubmed-2171942 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21719422008-03-05 Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 Faul, Christian Hüttelmaier, Stefan Oh, Jun Hachet, Virginie Singer, Robert H. Mundel, Peter J Cell Biol Research Articles 14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3-3 in mediating nuclear import has been described. There is also mounting evidence that nuclear import is regulated by the phosphorylation of cargo proteins, but the underlying mechanism remains elusive. Myopodin is a dual-compartment, actin-bundling protein that functions as a tumor suppressor in human bladder cancer. In muscle cells, myopodin redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. We show that importin α binding and the subsequent nuclear import of myopodin are regulated by the serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3. These results establish a novel paradigm for the promotion of nuclear import by 14-3-3 binding. They provide a molecular explanation for the phosphorylation-dependent nuclear import of nuclear localization signal-containing cargo proteins. The Rockefeller University Press 2005-05-09 /pmc/articles/PMC2171942/ /pubmed/15883195 http://dx.doi.org/10.1083/jcb.200411169 Text en Copyright © 2005, The Rockefeller University Press 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 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Faul, Christian Hüttelmaier, Stefan Oh, Jun Hachet, Virginie Singer, Robert H. Mundel, Peter Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title | Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title_full | Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title_fullStr | Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title_full_unstemmed | Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title_short | Promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
title_sort | promotion of importin α–mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3 |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171942/ https://www.ncbi.nlm.nih.gov/pubmed/15883195 http://dx.doi.org/10.1083/jcb.200411169 |
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