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Data on dimer formation between importin ? subtypes.

ABSTRACT: This article describes data related to the research article titled "Functional characterization of importin ?8 as a classical nuclear localization signal receptor" [1]. A GST pull-down assay showed that both importin ?1 and ?8, which are classical nuclear localization signal (cNLS) receptors, can form a dimer with importin ?6, ?7, or ?8. Importin ?8 has higher dimer-forming ability than importin ?1. In addition, our data show that either importin ?1 or importin ?8 can form a heterodimer with importin ?3, 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 ?3.

SUBMITTER: Miyamoto Y

PROVIDER: S-EPMC4865633 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Data on dimer formation between importin α subtypes.

Miyamoto Yoichi Y Oka Masahiro M

Data in brief 20160401

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 imp ...[more]

PMID: 27222842

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