ArticleMolecular and cellular biology2003
Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 98 citations in OpenAlex.
- The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025Review
- DAXX-dependent H3.3 deposition maintains myoblast cell identity independently of other histone chaperone complexes.iScience · 2025Article
- The Dynamic Regulation of Daxx-Mediated Transcriptional Inhibition by SUMO and PML NBs.International journal of molecular sciences · 2025Review
- Daxx and HIRA go viral - How chromatin remodeling complexes affect DNA virus infection.Tumour virus research · 2025Review
- Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases.International journal of molecular sciences · 2024Review
- Article
- HIPK1 Inhibition Protects against Pathological Cardiac Hypertrophy by Inhibiting the CREB-C/EBPβ Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- KSFinder-a knowledge graph model for link prediction of novel phosphorylated substrates of kinases.PeerJ · 2023Article
- SUMOylated PRC1 controls histone H3.3 deposition and genome integrity of embryonic heterochromatin.The EMBO journal · 2020Article
- Changes in Protein Phosphorylation during Salivary Gland Degeneration in Haemaphysalis longicornis.The Korean journal of parasitology · 2020Article
- DAXX in cancer: phenomena, processes, mechanisms and regulation.Nucleic acids research · 2019Review
- Identifying HIPK1 as Target of miR-22-3p Enhancing Recombinant Protein Production From HEK 293 Cell by Using Microarray and HTP siRNA Screen.Biotechnology journal · 2018Article
- The expression level and prognostic value of HIPK3 among non-small-cell lung cancer patients in China.OncoTargets and therapy · 2018Article
- Epigenetic Regulation of Glutamic Acid Decarboxylase 67 in a Hippocampal Circuit.Cerebral cortex (New York, N.Y. : 1991) · 2017Article
- Article
- An RNA interference screen identifies druggable regulators of MeCP2 stability.Science translational medicine · 2017Article
- Article
- Cell extrinsic alterations in splenic B cell maturation in Flt3-ligand knockout mice.Immunity, inflammation and disease · 2015Article
- Effect of tyrosine autophosphorylation on catalytic activity and subcellular localisation of homeodomain-interacting protein kinases (HIPK).Cell communication and signaling : CCS · 2015Article
- DNA damage-induced regulatory interplay between DAXX, p53, ATM kinase and Wip1 phosphatase.Cell cycle (Georgetown, Tex.) · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe an interaction between homeodomain-interacting protein kinase 1 (HIPK1) and Daxx, two transcriptional regulators important in transducing growth-regulatory signals. We demonstrate that HIPK1 is ubiquitously expressed in mice and humans and localizes predominantly to the nucleus. Daxx normally resides within the nucleus in promyelocytic leukemia protein (PML) oncogenic domains (PODs), where it physically interacts with PML. Under certain circumstances, Daxx is relocalized from PODs to chromatin, where it then acts as a transcriptional repressor through an association with histone deacetylase (HDAC1). We propose two novel mechanisms for regulating the activity of Daxx, both mediated by HIPK1. First, HIPK1 physically interacts with Daxx in cells and consequently relocalizes Daxx from PODs. Daxx relocalization disrupts its interaction with PML and augments its interaction with HDAC1, likely influencing Daxx activity. Although the relocalization of Daxx from PODs is phosphorylation independent, an active HIPK1 kinase domain is required, suggesting that HIPK1 autophosphorylation is important in this interaction. Second, HIPK1 phosphorylates Daxx on Ser 669, and phosphorylation of this site is important in modulating the ability of Daxx to function as a transcriptional repressor. Mutation of Daxx Ser 669 to Ala results in increased repression in three of four transcriptional reporters, suggesting that phosphorylation by HIPK1 diminishes Daxx transcriptional repression of specific promoters. Taken together, our results indicate that HIPK1 and Daxx collaborate in regulating transcription.
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