Protein interaction network of alternatively spliced NudCD1 isoforms

Abstract 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 expres...

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Autores principales:	Patrick Asselin-Mullen, Anaïs Chauvin, Marie-Line Dubois, Romain Drissi, Dominique Lévesque, François-Michel Boisvert
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4a45e38ddd7a446ea90abed6112fa704
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spelling	oai:doaj.org-article:4a45e38ddd7a446ea90abed6112fa7042021-12-02T15:06:21ZProtein interaction network of alternatively spliced NudCD1 isoforms10.1038/s41598-017-13441-w2045-2322https://doaj.org/article/4a45e38ddd7a446ea90abed6112fa7042017-10-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-13441-whttps://doaj.org/toc/2045-2322Abstract 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.Patrick Asselin-MullenAnaïs ChauvinMarie-Line DuboisRomain DrissiDominique LévesqueFrançois-Michel BoisvertNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Patrick Asselin-Mullen Anaïs Chauvin Marie-Line Dubois Romain Drissi Dominique Lévesque François-Michel Boisvert Protein interaction network of alternatively spliced NudCD1 isoforms
description	Abstract 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	article
author	Patrick Asselin-Mullen Anaïs Chauvin Marie-Line Dubois Romain Drissi Dominique Lévesque François-Michel Boisvert
author_facet	Patrick Asselin-Mullen Anaïs Chauvin Marie-Line Dubois Romain Drissi Dominique Lévesque François-Michel Boisvert
author_sort	Patrick Asselin-Mullen
title	Protein interaction network of alternatively spliced NudCD1 isoforms
title_short	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_sort	protein interaction network of alternatively spliced nudcd1 isoforms
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4a45e38ddd7a446ea90abed6112fa704
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Protein interaction network of alternatively spliced NudCD1 isoforms

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