ArticleJournal of cell science2000
The Dlx3 protein harbors basic residues required for nuclear localization, transcriptional activity and binding to Msx1.
Article in Journal of cell science, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- MAST4 regulates stem cell maintenance with DLX3 for epithelial development and amelogenesis.Experimental & molecular medicine · 2024Article
- Review
- Salt Dependence of DNA Binding Activity of Human Transcription Factor Dlx3.International journal of molecular sciences · 2022Article
- Protein localization screeningJournal of cell science · 2018Article
- DLX3 interacts with GCM1 and inhibits its transactivation-stimulating activity in a homeodomain-dependent manner in human trophoblast-derived cells.Scientific reports · 2017Article
- A novel DLX3-PKC integrated signaling network drives keratinocyte differentiation.Cell death and differentiation · 2017Article
- Alanine Expansions Associated with Congenital Central Hypoventilation Syndrome Impair PHOX2B Homeodomain-mediated Dimerization and Nuclear Import.The Journal of biological chemistry · 2016Article
- Clinical and functional data implicate the Arg(151)Ser variant of MSX1 in familial hypodontia.European journal of human genetics : EJHG · 2011Article
- SUMOylation of DLX3 by SUMO1 promotes its transcriptional activity.Journal of cellular biochemistry · 2011Article
- In vivo impact of a 4 bp deletion mutation in the DLX3 gene on bone development.Developmental biology · 2009Article
- Dlx3 is a crucial regulator of hair follicle differentiation and cycling.Development (Cambridge, England) · 2008Article
- Molecular consequences of a frameshifted DLX3 mutant leading to Tricho-Dento-Osseous syndrome.The Journal of biological chemistry · 2008Article
- Expression and function of Dlx genes in the osteoblast lineage.Developmental biology · 2008Article
- A 4 bp deletion mutation in DLX3 enhances osteoblastic differentiation and bone formation in vitro.Bone · 2008Article
- PAX9 and TGFB3 are linked to susceptibility to nonsyndromic cleft lip with or without cleft palate in the Japanese: population-based and family-based candidate gene analyses.Journal of human genetics · 2006Article
- Dlx genes, p63, and ectodermal dysplasias.Birth defects research. Part C, Embryo today : reviews · 2005Review
- Dlx3 transcriptional regulation of osteoblast differentiation: temporal recruitment of Msx2, Dlx3, and Dlx5 homeodomain proteins to chromatin of the osteocalcin gene.Molecular and cellular biology · 2004Article
- Complete sequencing shows a role for MSX1 in non-syndromic cleft lip and palate.Journal of medical genetics · 2003Article
- Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain.Molecular biology of the cell · 2003Article
- Phosphorylation of murine homeodomain protein Dlx3 by protein kinase C.FEBS letters · 2001Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The murine Dlx3 protein is a putative transcriptional activator that has been implicated during development and differentiation of epithelial tissue. Dlx3 contains a homeodomain and mutational analysis has revealed two regions, one N-terminal and one C-terminal to the homeodomain, that act as transcriptional activators in a yeast one-hybrid assay. In addition to transactivation, data are presented to demonstrate specific DNA binding and an association between Dlx3 and the Msx1 protein in vitro. Immunohistochemical analysis confirmed coexpression of Dlx3 and Msx1 proteins in the differentiated layers of murine epidermal tissues. Transcription factor function requires nuclear localization. In this study, the intracellular localization of the green fluorescent protein fused to Dlx3 was examined in keratinocytes induced to differentiate by calcium and is shown to localize to the nucleus. A bipartite nuclear localization signal (NLS) was identified by mutational analysis and shown to be sufficient for nuclear localization. This was demonstrated by insertion of the Dlx3 bipartite NLS sequence into a cytoplasmic fusion protein, GFP-keratin 14, which functionally redirected GFP-keratin 14 expression to the nucleus. Further analysis of Dlx3 NLS mutants revealed that the Dlx3 NLS sequences are required for specific DNA binding, transactivation potential and interactions with the Msx1 protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.