Protein interaction network of alternatively spliced NudCD1 isoforms
NudCD1, also known as CML66 or OVA66, is a protein initially identified as overexpressed in patients with chronic myelogenous leukemia. The mRNA of NudCD1 is expressed in heart and testis of normal tissues, and is overexpressed in several cancers. Previous studies have shown that the expression leve...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5636827/ https://www.ncbi.nlm.nih.gov/pubmed/29021621 http://dx.doi.org/10.1038/s41598-017-13441-w |
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author | Asselin-Mullen, Patrick Chauvin, Anaïs Dubois, Marie-Line Drissi, Romain Lévesque, Dominique Boisvert, François-Michel |
author_facet | Asselin-Mullen, Patrick Chauvin, Anaïs Dubois, Marie-Line Drissi, Romain Lévesque, Dominique Boisvert, François-Michel |
author_sort | Asselin-Mullen, Patrick |
collection | PubMed |
description | NudCD1, also known as CML66 or OVA66, is a protein initially identified as overexpressed in patients with chronic myelogenous leukemia. The mRNA of NudCD1 is expressed in heart and testis of normal tissues, and is overexpressed in several cancers. Previous studies have shown that the expression level of the protein correlates with tumoral phenotype, possibly interacting upstream of the Insulin Growth Factor - 1 Receptor (IGF-1R). The gene encoding the NudCD1 protein consists of 12 exons that can be alternative spliced, leading to the expression of three different isoforms. These isoforms possess a common region of 492 amino acids in their C-terminus region and have an isoform specific N-terminus. To determine the distinct function of each isoforms, we have localised the isoforms within the cells using immunofluorescence microscopy and used a quantitative proteomics approach (SILAC) to identify specific protein interaction partners for each isoforms. Localization studies showed a different subcellular distribution for the different isoforms, with the first isoform being nuclear, while the other two isoforms have distinct cytoplasmic and nuclear location. We found that the different NudCD1 isoforms have unique interacting partners, with the first isoform binding to a putative RNA helicase named DHX15 involved in mRNA splicing. |
format | Online Article Text |
id | pubmed-5636827 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56368272017-10-18 Protein interaction network of alternatively spliced NudCD1 isoforms Asselin-Mullen, Patrick Chauvin, Anaïs Dubois, Marie-Line Drissi, Romain Lévesque, Dominique Boisvert, François-Michel Sci Rep Article NudCD1, also known as CML66 or OVA66, is a protein initially identified as overexpressed in patients with chronic myelogenous leukemia. The mRNA of NudCD1 is expressed in heart and testis of normal tissues, and is overexpressed in several cancers. Previous studies have shown that the expression level of the protein correlates with tumoral phenotype, possibly interacting upstream of the Insulin Growth Factor - 1 Receptor (IGF-1R). The gene encoding the NudCD1 protein consists of 12 exons that can be alternative spliced, leading to the expression of three different isoforms. These isoforms possess a common region of 492 amino acids in their C-terminus region and have an isoform specific N-terminus. To determine the distinct function of each isoforms, we have localised the isoforms within the cells using immunofluorescence microscopy and used a quantitative proteomics approach (SILAC) to identify specific protein interaction partners for each isoforms. Localization studies showed a different subcellular distribution for the different isoforms, with the first isoform being nuclear, while the other two isoforms have distinct cytoplasmic and nuclear location. We found that the different NudCD1 isoforms have unique interacting partners, with the first isoform binding to a putative RNA helicase named DHX15 involved in mRNA splicing. Nature Publishing Group UK 2017-10-11 /pmc/articles/PMC5636827/ /pubmed/29021621 http://dx.doi.org/10.1038/s41598-017-13441-w Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Asselin-Mullen, Patrick Chauvin, Anaïs Dubois, Marie-Line Drissi, Romain Lévesque, Dominique Boisvert, François-Michel Protein interaction network of alternatively spliced NudCD1 isoforms |
title | Protein interaction network of alternatively spliced NudCD1 isoforms |
title_full | Protein interaction network of alternatively spliced NudCD1 isoforms |
title_fullStr | Protein interaction network of alternatively spliced NudCD1 isoforms |
title_full_unstemmed | Protein interaction network of alternatively spliced NudCD1 isoforms |
title_short | Protein interaction network of alternatively spliced NudCD1 isoforms |
title_sort | protein interaction network of alternatively spliced nudcd1 isoforms |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5636827/ https://www.ncbi.nlm.nih.gov/pubmed/29021621 http://dx.doi.org/10.1038/s41598-017-13441-w |
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