ArticleNucleic acids research2009
CK2 phosphorylation of the PRH/Hex homeodomain functions as a reversible switch for DNA binding.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Phosphorylation of GntR reduces Streptococcus suis oxidative stress resistance and virulence by inhibiting NADH oxidase transcription.PLoS pathogens · 2023Article
- Inhibition of Intimal Thickening By PRH (Proline-Rich Homeodomain) in Mice.Arteriosclerosis, thrombosis, and vascular biology · 2023Article
- The Haematopoietically-expressed homeobox transcription factor: roles in development, physiology and disease.Frontiers in immunology · 2023Review
- CK2-induced cooperation of HHEX with the YAP-TEAD4 complex promotes colorectal tumorigenesis.Nature communications · 2022Article
- CK2 and the Hallmarks of Cancer.Biomedicines · 2022Review
- Phosphorylation of NANOG by casein kinase I regulates embryonic stem cell self-renewal.FEBS letters · 2021Article
- Targeting protein kinase CK2 in the treatment of cholangiocarcinoma.Exploration of targeted anti-tumor therapy · 2021Review
- Identification and validation of the phosphorylation sites on Aristaless-related homeobox protein.Bioscience reports · 2020Article
- Blood platelets stimulate cancer extravasation through TGFβ-mediated downregulation of PRH/HHEX.Oncogenesis · 2020Article
- Protein kinase CK2 inhibition suppresses neointima formation via a proline-rich homeodomain-dependent mechanism.Vascular pharmacology · 2017Article
- Proline-Rich Homeodomain protein (PRH/HHEX) is a suppressor of breast tumour growth.Oncogenesis · 2017Article
- CK2 abrogates the inhibitory effects of PRH/HHEX on prostate cancer cell migration and invasion and acts through PRH to control cell proliferation.Oncogenesis · 2017Article
- Misregulation of the proline rich homeodomain (PRH/HHEX) protein in cancer cells and its consequences for tumour growth and invasion.Cell & bioscience · 2016Review
- PRH/HHex inhibits the migration of breast and prostate epithelial cells through direct transcriptional regulation of Endoglin.Oncogene · 2014Article
- CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.Journal of virology · 2013Article
- Dasatinib inhibits leukaemic cell survival by decreasing PRH/Hhex phosphorylation resulting in increased repression of VEGF signalling genes.Leukemia research · 2012Article
- Protein kinase CK2 inactivates PRH/Hhex using multiple mechanisms to de-repress VEGF-signalling genes and promote cell survival.Nucleic acids research · 2012Article
- The proline rich homeodomain protein PRH/Hhex forms stable oligomers that are highly resistant to denaturation.PloS one · 2012Article
- Karyopherins in nuclear transport of homeodomain proteins during development.Biochimica et biophysica acta · 2011Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The proline-rich homeodomain protein (PRH/Hex) regulates transcription by binding to specific DNA sequences and regulates mRNA transport by binding to translation initiation factor eIF4E. Protein kinase CK2 plays multiple roles in the regulation of gene expression and cell proliferation. Here, we show that PRH interacts with the beta subunit of CK2 in vitro and in cells and that CK2 phosphorylates PRH. Phosphorylation of PRH by CK2 inhibits the DNA binding activity of this protein and dephosphorylation restores DNA binding indicating that this modification acts as a reversible switch. We show that phosphorylation of the homeodomain is sufficient to block DNA binding and we identify two amino acids within this the domain that are phosphorylated by CK2: S163 and S177. Site-directed mutagenesis demonstrates that mutation of either of these residues to glutamic acid partially mimics phosphorylation but is insufficient to completely block DNA binding whereas an S163E/S177E double mutation severely inhibits DNA binding. Significantly, the S163E and S177E mutations and the S163E/S177E double mutation all inhibit the ability of PRH to regulate transcription in cells. Since these amino acids are conserved between many homeodomain proteins, our results suggest that CK2 may regulate the activity of several homeodomain proteins in this manner.
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Registered trials
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