ArticleThe Journal of biological chemistry2009
Importin 13 mediates nuclear import of histone fold-containing chromatin accessibility complex heterodimers.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Fuzzy Interactions Form and Shape the Histone Transport Complex.Molecular cell · 2019Article
- Extensive Identification and In-depth Validation of Importin 13 Cargoes.Molecular & cellular proteomics : MCP · 2018Article
- Extensive cargo identification reveals distinct biological roles of the 12 importin pathways.eLife · 2017Article
- CCCTC-binding factor controls its own nuclear transport via regulating the expression of importin 13.Molecules and cells · 2013Article
- Structural basis for the nuclear export activity of Importin13.The EMBO journal · 2013Article
- Nuclear import by karyopherin-βs: recognition and inhibition.Biochimica et biophysica acta · 2011Review
- Ran-dependent nuclear export mediators: a structural perspective.The EMBO journal · 2011Review
- Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation.The EMBO journal · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The histone fold is a structural element that facilitates heterodimerization, and histone fold heterodimers play crucial roles in gene regulation. Here, we investigated the nuclear import of two human histone fold pairs, which belong to the H2A/H2B family: CHRAC-15/CHRAC-17 and p12/CHRAC-17. Our results from in vitro nuclear import assays with permeabilized cells and in vivo cotransfection experiments reveal that importin 13 facilitates nuclear import of both histone fold heterodimers. Using glutathione S-transferase pulldown experiments, we provide evidence that heterodimers are required for efficient binding of importin 13 because the monomers alone do not significantly interact. Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17. The distribution of basic amino acid residues among the histone fold subunits essential for nuclear uptake suggests that heterodimerization of the histone fold motif-containing proteins forms an importin 13-specific binding platform.
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Registered trials
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