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...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2016-06-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340916301883 |
| _version_ | 1818505493739470848 |
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| author | Yoichi Miyamoto Masahiro Oka |
| author_facet | Yoichi Miyamoto Masahiro Oka |
| author_sort | Yoichi Miyamoto |
| collection | DOAJ |
| 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. Keywords: Nuclear transport, Importin α, Nuclear localization signal, Dimer |
| first_indexed | 2024-12-10T21:51:32Z |
| format | Article |
| id | doaj.art-256dd5248e3844f68f758739dd8e2425 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-10T21:51:32Z |
| publishDate | 2016-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-256dd5248e3844f68f758739dd8e24252022-12-22T01:32:11ZengElsevierData in Brief2352-34092016-06-01712481253Data on dimer formation between importin α subtypesYoichi Miyamoto0Masahiro Oka1Laboratory of Nuclear Transport Dynamics, National Institutes of Biomedical Innovation, Health and Nutrition, 7-6-8 Saito-Asagi, Ibaraki, Osaka 567-0085, JapanLaboratory of Nuclear Transport Dynamics, National Institutes of Biomedical Innovation, Health and Nutrition, 7-6-8 Saito-Asagi, Ibaraki, Osaka 567-0085, JapanThis 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. Keywords: Nuclear transport, Importin α, Nuclear localization signal, Dimerhttp://www.sciencedirect.com/science/article/pii/S2352340916301883 |
| spellingShingle | Yoichi Miyamoto Masahiro Oka Data on dimer formation between importin α subtypes Data in Brief |
| 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 |
| url | http://www.sciencedirect.com/science/article/pii/S2352340916301883 |
| work_keys_str_mv | AT yoichimiyamoto dataondimerformationbetweenimportinasubtypes AT masahirooka dataondimerformationbetweenimportinasubtypes |