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Intranuclear dynamics of the Nup107-160 complex
Nup98 is a glycine-leucine-phenylalanine-glycine (GLFG) repeat–containing nucleoporin that, in addition to nuclear transport, contributes to multiple aspects of gene regulation. Previous studies revealed its dynamic localization within intranuclear structures known as GLFG bodies. Here we show that...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4462950/ https://www.ncbi.nlm.nih.gov/pubmed/25904327 http://dx.doi.org/10.1091/mbc.E15-02-0060 |
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author | Morchoisne-Bolhy, Stéphanie Geoffroy, Marie-Claude Bouhlel, Imène B. Alves, Annabelle Audugé, Nicolas Baudin, Xavier Van Bortle, Kevin Powers, Maureen A. Doye, Valérie |
author_facet | Morchoisne-Bolhy, Stéphanie Geoffroy, Marie-Claude Bouhlel, Imène B. Alves, Annabelle Audugé, Nicolas Baudin, Xavier Van Bortle, Kevin Powers, Maureen A. Doye, Valérie |
author_sort | Morchoisne-Bolhy, Stéphanie |
collection | PubMed |
description | Nup98 is a glycine-leucine-phenylalanine-glycine (GLFG) repeat–containing nucleoporin that, in addition to nuclear transport, contributes to multiple aspects of gene regulation. Previous studies revealed its dynamic localization within intranuclear structures known as GLFG bodies. Here we show that the mammalian Nup107-160 complex (Y-complex), a major scaffold module of the nuclear pore, together with its partner Elys, colocalizes with Nup98 in GLFG bodies. The frequency and size of GLFG bodies vary among HeLa sublines, and we find that an increased level of Nup98 is associated with the presence of bodies. Recruitment of the Y-complex and Elys into GLFG bodies requires the C-terminal domain of Nup98. During cell division, Y-Nup–containing GLFG bodies are disassembled in mitotic prophase, significantly ahead of nuclear pore disassembly. FRAP studies revealed that, unlike at nuclear pores, the Y-complex shuttles into and out of GLFG bodies. Finally, we show that within the nucleoplasm, a fraction of Nup107, a key component of the Y-complex, displays reduced mobility, suggesting interaction with other nuclear components. Together our data uncover a previously neglected intranuclear pool of the Y-complex that may underscore a yet-uncharacterized function of these nucleoporins inside the nucleus, even in cells that contain no detectable GLFG bodies. |
format | Online Article Text |
id | pubmed-4462950 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-44629502015-08-30 Intranuclear dynamics of the Nup107-160 complex Morchoisne-Bolhy, Stéphanie Geoffroy, Marie-Claude Bouhlel, Imène B. Alves, Annabelle Audugé, Nicolas Baudin, Xavier Van Bortle, Kevin Powers, Maureen A. Doye, Valérie Mol Biol Cell Articles Nup98 is a glycine-leucine-phenylalanine-glycine (GLFG) repeat–containing nucleoporin that, in addition to nuclear transport, contributes to multiple aspects of gene regulation. Previous studies revealed its dynamic localization within intranuclear structures known as GLFG bodies. Here we show that the mammalian Nup107-160 complex (Y-complex), a major scaffold module of the nuclear pore, together with its partner Elys, colocalizes with Nup98 in GLFG bodies. The frequency and size of GLFG bodies vary among HeLa sublines, and we find that an increased level of Nup98 is associated with the presence of bodies. Recruitment of the Y-complex and Elys into GLFG bodies requires the C-terminal domain of Nup98. During cell division, Y-Nup–containing GLFG bodies are disassembled in mitotic prophase, significantly ahead of nuclear pore disassembly. FRAP studies revealed that, unlike at nuclear pores, the Y-complex shuttles into and out of GLFG bodies. Finally, we show that within the nucleoplasm, a fraction of Nup107, a key component of the Y-complex, displays reduced mobility, suggesting interaction with other nuclear components. Together our data uncover a previously neglected intranuclear pool of the Y-complex that may underscore a yet-uncharacterized function of these nucleoporins inside the nucleus, even in cells that contain no detectable GLFG bodies. The American Society for Cell Biology 2015-06-15 /pmc/articles/PMC4462950/ /pubmed/25904327 http://dx.doi.org/10.1091/mbc.E15-02-0060 Text en © 2015 Morchoisne-Bolhy et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Morchoisne-Bolhy, Stéphanie Geoffroy, Marie-Claude Bouhlel, Imène B. Alves, Annabelle Audugé, Nicolas Baudin, Xavier Van Bortle, Kevin Powers, Maureen A. Doye, Valérie Intranuclear dynamics of the Nup107-160 complex |
title | Intranuclear dynamics of the Nup107-160 complex |
title_full | Intranuclear dynamics of the Nup107-160 complex |
title_fullStr | Intranuclear dynamics of the Nup107-160 complex |
title_full_unstemmed | Intranuclear dynamics of the Nup107-160 complex |
title_short | Intranuclear dynamics of the Nup107-160 complex |
title_sort | intranuclear dynamics of the nup107-160 complex |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4462950/ https://www.ncbi.nlm.nih.gov/pubmed/25904327 http://dx.doi.org/10.1091/mbc.E15-02-0060 |
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