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The nucleoporin Nup88 is interacting with nuclear lamin A

Nuclear pore complexes (NPCs) are embedded in the nuclear envelope (NE) and mediate bidirectional nucleocytoplasmic transport. Their spatial distribution in the NE is organized by the nuclear lamina, a meshwork of nuclear intermediate filament proteins. Major constituents of the nuclear lamina are A...

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Autores principales: Lussi, Yvonne C., Hügi, Ilona, Laurell, Eva, Kutay, Ulrike, Fahrenkrog, Birthe
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3069011/
https://www.ncbi.nlm.nih.gov/pubmed/21289091
http://dx.doi.org/10.1091/mbc.E10-05-0463
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author Lussi, Yvonne C.
Hügi, Ilona
Laurell, Eva
Kutay, Ulrike
Fahrenkrog, Birthe
author_facet Lussi, Yvonne C.
Hügi, Ilona
Laurell, Eva
Kutay, Ulrike
Fahrenkrog, Birthe
author_sort Lussi, Yvonne C.
collection PubMed
description Nuclear pore complexes (NPCs) are embedded in the nuclear envelope (NE) and mediate bidirectional nucleocytoplasmic transport. Their spatial distribution in the NE is organized by the nuclear lamina, a meshwork of nuclear intermediate filament proteins. Major constituents of the nuclear lamina are A- and B-type lamins. In this work we show that the nuclear pore protein Nup88 binds lamin A in vitro and in vivo. The interaction is mediated by the N-terminus of Nup88, and Nup88 specifically binds the tail domain of lamin A but not of lamins B1 and B2. Expression of green fluorescent protein–tagged lamin A in cells causes a masking of binding sites for Nup88 antibodies in immunofluorescence assays, supporting the interaction of lamin A with Nup88 in a cellular context. The epitope masking disappears in cells expressing mutants of lamin A that are associated with laminopathic diseases. Consistently, an interaction of Nup88 with these mutants is disrupted in vitro. Immunoelectron microscopy using Xenopus laevis oocyte nuclei further revealed that Nup88 localizes to the cytoplasmic and nuclear face of the NPC. Together our data suggest that a pool of Nup88 on the nuclear side of the NPC provides a novel, unexpected binding site for nuclear lamin A.
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spelling pubmed-30690112011-06-16 The nucleoporin Nup88 is interacting with nuclear lamin A Lussi, Yvonne C. Hügi, Ilona Laurell, Eva Kutay, Ulrike Fahrenkrog, Birthe Mol Biol Cell Articles Nuclear pore complexes (NPCs) are embedded in the nuclear envelope (NE) and mediate bidirectional nucleocytoplasmic transport. Their spatial distribution in the NE is organized by the nuclear lamina, a meshwork of nuclear intermediate filament proteins. Major constituents of the nuclear lamina are A- and B-type lamins. In this work we show that the nuclear pore protein Nup88 binds lamin A in vitro and in vivo. The interaction is mediated by the N-terminus of Nup88, and Nup88 specifically binds the tail domain of lamin A but not of lamins B1 and B2. Expression of green fluorescent protein–tagged lamin A in cells causes a masking of binding sites for Nup88 antibodies in immunofluorescence assays, supporting the interaction of lamin A with Nup88 in a cellular context. The epitope masking disappears in cells expressing mutants of lamin A that are associated with laminopathic diseases. Consistently, an interaction of Nup88 with these mutants is disrupted in vitro. Immunoelectron microscopy using Xenopus laevis oocyte nuclei further revealed that Nup88 localizes to the cytoplasmic and nuclear face of the NPC. Together our data suggest that a pool of Nup88 on the nuclear side of the NPC provides a novel, unexpected binding site for nuclear lamin A. The American Society for Cell Biology 2011-04-01 /pmc/articles/PMC3069011/ /pubmed/21289091 http://dx.doi.org/10.1091/mbc.E10-05-0463 Text en © 2011 Lussi 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 of Cell Biology.
spellingShingle Articles
Lussi, Yvonne C.
Hügi, Ilona
Laurell, Eva
Kutay, Ulrike
Fahrenkrog, Birthe
The nucleoporin Nup88 is interacting with nuclear lamin A
title The nucleoporin Nup88 is interacting with nuclear lamin A
title_full The nucleoporin Nup88 is interacting with nuclear lamin A
title_fullStr The nucleoporin Nup88 is interacting with nuclear lamin A
title_full_unstemmed The nucleoporin Nup88 is interacting with nuclear lamin A
title_short The nucleoporin Nup88 is interacting with nuclear lamin A
title_sort nucleoporin nup88 is interacting with nuclear lamin a
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3069011/
https://www.ncbi.nlm.nih.gov/pubmed/21289091
http://dx.doi.org/10.1091/mbc.E10-05-0463
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