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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...

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Autores principales: Faul, Christian, Hüttelmaier, Stefan, Oh, Jun, Hachet, Virginie, Singer, Robert H., Mundel, Peter
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
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.
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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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