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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...

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Autores principales: Morchoisne-Bolhy, Stéphanie, Geoffroy, Marie-Claude, Bouhlel, Imène B., Alves, Annabelle, Audugé, Nicolas, Baudin, Xavier, Van Bortle, Kevin, Powers, Maureen A., Doye, Valérie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
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.
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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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