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Galectin-3 interacts with components of the nuclear ribonucleoprotein complex

BACKGROUND: The multifunctional β-galactoside-binding protein galectin-3 is found in many distinct subcellular compartments including the cell nucleus. Expression and distribution of galectin-3 between the cell nucleus and the cytosol changes during cell differentiation and cancer development. Nucle...

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Autores principales: Fritsch, Katharina, Mernberger, Marco, Nist, Andrea, Stiewe, Thorsten, Brehm, Alexander, Jacob, Ralf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4952364/
https://www.ncbi.nlm.nih.gov/pubmed/27435226
http://dx.doi.org/10.1186/s12885-016-2546-0
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author Fritsch, Katharina
Mernberger, Marco
Nist, Andrea
Stiewe, Thorsten
Brehm, Alexander
Jacob, Ralf
author_facet Fritsch, Katharina
Mernberger, Marco
Nist, Andrea
Stiewe, Thorsten
Brehm, Alexander
Jacob, Ralf
author_sort Fritsch, Katharina
collection PubMed
description BACKGROUND: The multifunctional β-galactoside-binding protein galectin-3 is found in many distinct subcellular compartments including the cell nucleus. Expression and distribution of galectin-3 between the cell nucleus and the cytosol changes during cell differentiation and cancer development. Nuclear functions of galectin-3 and how they contribute to tumorigenesis are not understood. METHODS: In order to identify nuclear galectin-3 interaction partners, we used affinity chromatography and co-immunoprecipitation. Spatial proximity in the nucleus was assessed by immunofluorescence and proximity ligation assay. We also investigated the function of galectin-3 on mRNA-export by fluorescence in situ hybridization and on mRNA-processing by RNA-sequencing. RESULTS: The heterogeneous ribonucleoprotein particle component hnRNPA2B1 was identified as a novel galectin-3 binding protein that associates with the lectin in a lactose-dependent manner in the cell nucleus. Specific individual depletion of galectin-3 does not affect the mRNA distribution between cytoplasm and nucleus. A significant alteration of this distribution was observed after combined depletion of galectin-1 and −3. However, silencing of galectin-3 was sufficient to alter the splicing patterns of several genes. CONCLUSIONS: Galectin-3 and hnRNPA2B1 interact as members of the early splicing machinery. Galectin-3 and −1 have redundant functions in mRNA transport and at least in part in mRNA splicing. RNA-sequencing data points to a specific function of the hnRNPA2B1/galectin-3 interaction in the processing of transcripts coding for the nuclear oncoprotein SET. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12885-016-2546-0) contains supplementary material, which is available to authorized users.
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spelling pubmed-49523642016-07-21 Galectin-3 interacts with components of the nuclear ribonucleoprotein complex Fritsch, Katharina Mernberger, Marco Nist, Andrea Stiewe, Thorsten Brehm, Alexander Jacob, Ralf BMC Cancer Research Article BACKGROUND: The multifunctional β-galactoside-binding protein galectin-3 is found in many distinct subcellular compartments including the cell nucleus. Expression and distribution of galectin-3 between the cell nucleus and the cytosol changes during cell differentiation and cancer development. Nuclear functions of galectin-3 and how they contribute to tumorigenesis are not understood. METHODS: In order to identify nuclear galectin-3 interaction partners, we used affinity chromatography and co-immunoprecipitation. Spatial proximity in the nucleus was assessed by immunofluorescence and proximity ligation assay. We also investigated the function of galectin-3 on mRNA-export by fluorescence in situ hybridization and on mRNA-processing by RNA-sequencing. RESULTS: The heterogeneous ribonucleoprotein particle component hnRNPA2B1 was identified as a novel galectin-3 binding protein that associates with the lectin in a lactose-dependent manner in the cell nucleus. Specific individual depletion of galectin-3 does not affect the mRNA distribution between cytoplasm and nucleus. A significant alteration of this distribution was observed after combined depletion of galectin-1 and −3. However, silencing of galectin-3 was sufficient to alter the splicing patterns of several genes. CONCLUSIONS: Galectin-3 and hnRNPA2B1 interact as members of the early splicing machinery. Galectin-3 and −1 have redundant functions in mRNA transport and at least in part in mRNA splicing. RNA-sequencing data points to a specific function of the hnRNPA2B1/galectin-3 interaction in the processing of transcripts coding for the nuclear oncoprotein SET. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12885-016-2546-0) contains supplementary material, which is available to authorized users. BioMed Central 2016-07-19 /pmc/articles/PMC4952364/ /pubmed/27435226 http://dx.doi.org/10.1186/s12885-016-2546-0 Text en © The Author(s). 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Fritsch, Katharina
Mernberger, Marco
Nist, Andrea
Stiewe, Thorsten
Brehm, Alexander
Jacob, Ralf
Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title_full Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title_fullStr Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title_full_unstemmed Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title_short Galectin-3 interacts with components of the nuclear ribonucleoprotein complex
title_sort galectin-3 interacts with components of the nuclear ribonucleoprotein complex
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4952364/
https://www.ncbi.nlm.nih.gov/pubmed/27435226
http://dx.doi.org/10.1186/s12885-016-2546-0
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