ArticleMolecular and cellular biology1999
Identification of the in vivo casein kinase II phosphorylation site within the homeodomain of the cardiac tisue-specifying homeobox gene product Csx/Nkx2.5.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 89 citations in OpenAlex.
- Smad4 regulates the nuclear translocation of Nkx2-5 in cardiac differentiation.Scientific reports · 2021Article
- Phosphorylation of NANOG by casein kinase I regulates embryonic stem cell self-renewal.FEBS letters · 2021Article
- Crystal Structures of Ternary Complexes of MEF2 and NKX2-5 Bound to DNA Reveal a Disease Related Protein-Protein Interaction Interface.Journal of molecular biology · 2020Article
- Nkx2-5 Regulates the Proliferation and Migration of H9c2 Cells.Medical science monitor : international medical journal of experimental and clinical research · 2020Article
- Identification and validation of the phosphorylation sites on Aristaless-related homeobox protein.Bioscience reports · 2020Article
- Analysis of NKX2-5 in 439 Chinese Patients with Sporadic Atrial Septal Defect.Medical science monitor : international medical journal of experimental and clinical research · 2019Article
- A comprehensive in silico analysis, distribution and frequency of humanJournal of cardiovascular and thoracic research · 2019Article
- Mechanism Sharing Between Genetic and Gestational Hypoxia-Induced Cardiac Anomalies.Frontiers in cardiovascular medicine · 2018Article
- Fractal heterogeneity in minimal matrix models of scars modulates stiff-niche stem-cell responses via nuclear exit of a mechanorepressor.Nature materials · 2015Article
- Article
- NKX2-5 mutations in an inbred consanguineous population: genetic and phenotypic diversity.Scientific reports · 2015Article
- Phosphorylation of Shox2 is required for its function to control sinoatrial node formation.Journal of the American Heart Association · 2014Article
- Functional characterization of a novel mutation in NKX2-5 associated with congenital heart disease and adult-onset cardiomyopathy.Circulation. Cardiovascular genetics · 2013Article
- Article
- Ischemia-reperfusion injury and pregnancy initiate time-dependent and robust signs of up-regulation of cardiac progenitor cells.PloS one · 2012Article
- Cardiac transcription factor Nkx2.5 is downregulated under excessive O-GlcNAcylation condition.PloS one · 2012Article
- Karyopherins in nuclear transport of homeodomain proteins during development.Biochimica et biophysica acta · 2011Review
- The representation of heart development in the gene ontology.Developmental biology · 2011Article
- Molecular characterization, expression patterns and polymorphism analysis of porcine Six1 gene.Molecular biology reports · 2011Article
- Expression of sumoylation deficient Nkx2.5 mutant in Nkx2.5 haploinsufficient mice leads to congenital heart defects.PloS one · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Csx/Nkx2.5, a member of the homeodomain-containing transcription factors, serves critical developmental functions in heart formation in vertebrates and nonvertebrates. In this study the putative nuclear localization signal (NLS) of Csx/Nkx2.5 was identified by site-directed mutagenesis to the amino terminus of the homeodomain, which is conserved in almost all homeodomain proteins. When the putative NLS of Csx/Nkx2.5 was mutated a significant amount of the cytoplasmically localized Csx/Nkx2.5 was unphosphorylated, in contrast to the nuclearly localized Csx/Nkx2.5, which is serine- and threonine-phosphorylated, suggesting that Csx/Nkx2.5 phosphorylation is regulated, at least in part, by intracellular localization. Tryptic phosphopeptide mapping indicated that Csx/Nkx2.5 has at least five phosphorylation sites. Using in-gel kinase assays, we detected a Csx/Nkx2.5 kinase whose molecular mass is approximately 40 kDa in both cytoplasmic and nuclear extracts. Mutational analysis and in vitro kinase assays suggested that this 40-kDa Csx/Nkx2.5 kinase is a catalytic subunit of casein kinase II (CKII) that phosphorylates the serine residue between the first and second helix of the homeodomain. This CKII site is phosphorylated in vivo. CKII-dependent phosphorylation of the homeodomain increased Csx/Nkx2. 5 DNA binding. Serine-to-alanine mutation at the CKII phosphorylation site reduced transcriptional activity when the carboxyl-terminal repressor domain was deleted. Although the precise biological function of Csx/Nkx2.5 phosphorylation by CKII remains to be determined, it may play an important role, as this CKII phosphorylation site within the homeodomain is fully conserved in all known members of the NK2 family of the homeobox genes.
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