ArticleMolecular and cellular biology2002
Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- A covalent PFKL activator suppresses tumor growth.Nature chemical biology · 2026Article
- A Covalent PFKL Activator Suppresses Tumor Growth.bioRxiv : the preprint server for biology · 2025Article
- An evolutionarily distinct Hmgn2 variant influences shape recognition in Medaka Fish.Communications biology · 2024Article
- Article
- Shaking up the silence: consequences of HMGN1 antagonizing PRC2 in the Down syndrome brain.Epigenetics & chromatin · 2022Review
- Chromatin regulates IL-33 release and extracellular cytokine activity.Nature communications · 2018Article
- Real-time monitoring of PtaHMGB activity in poplar transactivation assays.Plant methods · 2017Article
- Growth Cone Localization of the mRNA Encoding the Chromatin Regulator HMGN5 Modulates Neurite Outgrowth.Molecular and cellular biology · 2015Article
- High mobility group nucleosomal binding domain 2 (HMGN2) SUMOylation by the SUMO E3 ligase PIAS1 decreases the binding affinity to nucleosome core particles.The Journal of biological chemistry · 2014Article
- Visualization of the expression of HMGN nucleosomal binding proteins in the developing mouse embryo and in adult mouse tissues.Methods in molecular biology (Clifton, N.J.) · 2009Article
- High mobility group proteins and their post-translational modifications.Biochimica et biophysica acta · 2008Review
- Cell cycle-dependent binding of HMGN proteins to chromatin.Molecular biology of the cell · 2008Article
- Delineation of the protein module that anchors HMGN proteins to nucleosomes in the chromatin of living cells.Molecular and cellular biology · 2008Article
- Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions.Molecular biology of the cell · 2005Article
- Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin.Molecular and cellular biology · 2004Article
- Chromosomal protein HMGN1 enhances the rate of DNA repair in chromatin.The EMBO journal · 2003Article
- Transcriptional regulation by HMGN proteins.Biochimica et biophysica actaReview
- HMG modifications and nuclear function.Biochimica et biophysica actaReview
- Nuclear functions of the HMG proteins.Biochimica et biophysica actaReview
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Progression through mitosis is associated with reversible phosphorylation of many nuclear proteins including that of the high-mobility group N (HMGN) nucleosomal binding protein family. Here we use immunofluorescence and in vitro nuclear import studies to demonstrate that mitotic phosphorylation of the nucleosomal binding domain (NBD) of the HMGN1 protein prevents its reentry into the newly formed nucleus in late telophase. By microinjecting wild-type and mutant proteins into the cytoplasm of HeLa cells and expressing these proteins in HmgN1(-/-) cells, we demonstrate that the inability to enter the nucleus is a consequence of phosphorylation and is not due to the presence of negative charges. Using affinity chromatography with recombinant proteins and nuclear extracts prepared from logarithmically growing or mitotically arrested cells, we demonstrate that phosphorylation of the NBD of HMGN1 promotes interaction with specific 14.3.3 isotypes. We conclude that mitotic phosphorylation of HMGN1 protein promotes interaction with 14.3.3 proteins and suggest that this interaction impedes the reentry of the proteins into the nucleus during telophase. Taken together with the results of previous studies, our results suggest a dual role for mitotic phosphorylation of HMGN1: abolishment of chromatin binding and inhibition of nuclear import.
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