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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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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. |
format | Online Article Text |
id | pubmed-4865633 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT miyamotoyoichi dataondimerformationbetweenimportinasubtypes AT okamasahiro dataondimerformationbetweenimportinasubtypes |