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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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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. |
format | Online Article Text |
id | pubmed-4952364 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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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