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Data on dimer formation between importin α subtypes

This article describes data related to the research article titled “Functional characterization of importin α8 as a classical nuclear localization signal receptor” [1]. A GST pull-down assay showed that both importin α1 and α8, which are classical nuclear localization signal (cNLS) receptors, can fo...

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Detalles Bibliográficos
Autores principales: Miyamoto, Yoichi, Oka, Masahiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4865633/
https://www.ncbi.nlm.nih.gov/pubmed/27222842
http://dx.doi.org/10.1016/j.dib.2016.03.080
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author Miyamoto, Yoichi
Oka, Masahiro
author_facet Miyamoto, Yoichi
Oka, Masahiro
author_sort Miyamoto, Yoichi
collection PubMed
description This article describes data related to the research article titled “Functional characterization of importin α8 as a classical nuclear localization signal receptor” [1]. A GST pull-down assay showed that both importin α1 and α8, which are classical nuclear localization signal (cNLS) receptors, can form a dimer with importin α6, α7, or α8. Importin α8 has higher dimer-forming ability than importin α1. In addition, our data show that either importin α1 or importin α8 can form a heterodimer with importin α3, which exists in a preformed complex with cNLS substrates such as the conventional SV40TNLS or the p53 protein, resulting in the release of the cNLS substrates from importin α3.
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spelling pubmed-48656332016-05-24 Data on dimer formation between importin α subtypes Miyamoto, Yoichi Oka, Masahiro Data Brief Data Article This article describes data related to the research article titled “Functional characterization of importin α8 as a classical nuclear localization signal receptor” [1]. A GST pull-down assay showed that both importin α1 and α8, which are classical nuclear localization signal (cNLS) receptors, can form a dimer with importin α6, α7, or α8. Importin α8 has higher dimer-forming ability than importin α1. In addition, our data show that either importin α1 or importin α8 can form a heterodimer with importin α3, which exists in a preformed complex with cNLS substrates such as the conventional SV40TNLS or the p53 protein, resulting in the release of the cNLS substrates from importin α3. Elsevier 2016-04-01 /pmc/articles/PMC4865633/ /pubmed/27222842 http://dx.doi.org/10.1016/j.dib.2016.03.080 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Miyamoto, Yoichi
Oka, Masahiro
Data on dimer formation between importin α subtypes
title Data on dimer formation between importin α subtypes
title_full Data on dimer formation between importin α subtypes
title_fullStr Data on dimer formation between importin α subtypes
title_full_unstemmed Data on dimer formation between importin α subtypes
title_short Data on dimer formation between importin α subtypes
title_sort data on dimer formation between importin α subtypes
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4865633/
https://www.ncbi.nlm.nih.gov/pubmed/27222842
http://dx.doi.org/10.1016/j.dib.2016.03.080
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