BIOMAT Database Logo BIOMAT Database Logo

Fos family members successively occupy the tyrosine hydroxylase gene AP-1 site after nerve growth factor or epidermal growth factor stimulation and can repress transcription. 1994

E Gizang-Ginsberg, and E B Ziff
Howard Hughes Medical Institute, Department of Biochemistry, New York University Medical Center, New York 10016.

Nerve growth factor induces the neuronal-like differentiation of PC12 cells, and epidermal growth factor promotes PC12 viability and is weakly mitogenic. Despite these differences, both growth factors induce indistinguishable patterns of transient delayed transcription of the tyrosine hydroxylase (TH) gene and the expression of proteins encoded by Fos gene family members. Thus, TH expression is sensitive to signaling pathways common to these two growth factors. We show that c-fos and fosB successively occupy an AP-1 site-like element of the TH promoter after nerve growth factor treatment. Furthermore, under conditions of transient transfection, Fos family proteins may synergize with c-jun to transrepress TH gene transcription through the TH-fat-specific element. We show that the target of repression is the AP-1 site-like element that lies within the TH-fat-specific element. We demonstrate that this site is also a major positive acting site for TH control. These results suggest a model in which the long term effect of c-fos family protein expression is to limit the expression of the TH gene. We consider the novel properties of this element in providing temporal and cell type-specific regulation of TH transcription.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009414 Nerve Growth Factors Factors which enhance the growth potentialities of sensory and sympathetic nerve cells. Neurite Outgrowth Factor,Neurite Outgrowth Factors,Neuronal Growth-Associated Protein,Neuronotrophic Factor,Neurotrophic Factor,Neurotrophic Factors,Neurotrophin,Neurotrophins,Growth-Associated Proteins, Neuronal,Neuronal Growth-Associated Proteins,Neuronotrophic Factors,Neurotrophic Protein,Neurotrophic Proteins,Proteins, Neuronal Growth-Associated,Factor, Neurite Outgrowth,Factor, Neuronotrophic,Factor, Neurotrophic,Factors, Nerve Growth,Factors, Neurite Outgrowth,Factors, Neuronotrophic,Factors, Neurotrophic,Growth Associated Proteins, Neuronal,Growth-Associated Protein, Neuronal,Neuronal Growth Associated Protein,Neuronal Growth Associated Proteins,Outgrowth Factor, Neurite,Outgrowth Factors, Neurite,Protein, Neuronal Growth-Associated
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone
D005786 Gene Expression Regulation Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation. Gene Action Regulation,Regulation of Gene Expression,Expression Regulation, Gene,Regulation, Gene Action,Regulation, Gene Expression
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014157 Transcription Factors Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. Transcription Factor,Factor, Transcription,Factors, Transcription
D014158 Transcription, Genetic The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION. Genetic Transcription
D014446 Tyrosine 3-Monooxygenase An enzyme that catalyzes the conversion of L-tyrosine, tetrahydrobiopterin, and oxygen to 3,4-dihydroxy-L-phenylalanine, dihydrobiopterin, and water. EC 1.14.16.2. Tyrosine Hydroxylase,3-Monooxygenase, Tyrosine,Hydroxylase, Tyrosine,Tyrosine 3 Monooxygenase

Related Publications

E Gizang-Ginsberg, and E B Ziff
AP-1, CREB and CBP transcription factors differentially regulate the tyrosine hydroxylase gene.
March 1998, Brain research. Molecular brain research,
E Gizang-Ginsberg, and E B Ziff
Common DNA binding site for Fos protein complexes and transcription factor AP-1.
February 1988, Cell,
E Gizang-Ginsberg, and E B Ziff
Regulated expression of the tyrosine hydroxylase gene by epidermal growth factor.
September 1987, Molecular and cellular biology,
E Gizang-Ginsberg, and E B Ziff
Regulation of tyrosine hydroxylase gene expression during transdifferentiation of striatal neurons: changes in transcription factors binding the AP-1 site.
October 1998, The Journal of neuroscience : the official journal of the Society for Neuroscience,
E Gizang-Ginsberg, and E B Ziff
Role of c-fos in hypoxia-induced AP-1 cis-element activity and tyrosine hydroxylase gene expression.
August 1998, Brain research. Molecular brain research,
E Gizang-Ginsberg, and E B Ziff
Cooperative stimulation of specific gene transcription by epidermal growth factor and transforming growth factor type beta 1.
February 1990, The Journal of biological chemistry,
E Gizang-Ginsberg, and E B Ziff
Regulation of the tyrosine hydroxylase and dopamine beta-hydroxylase genes by the transcription factor AP-2.
January 2001, Journal of neurochemistry,
E Gizang-Ginsberg, and E B Ziff
Nerve growth factor- and epidermal growth factor-regulated gene transcription in PC12 pheochromocytoma and INS-1 insulinoma cells.
December 2000, European journal of cell biology,
E Gizang-Ginsberg, and E B Ziff
Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells.
December 1990, The Journal of biological chemistry,
E Gizang-Ginsberg, and E B Ziff
The product of a fos-related gene, fra-1, binds cooperatively to the AP-1 site with Jun: transcription factor AP-1 is comprised of multiple protein complexes.
February 1989, Genes & development,
Copied contents to your clipboard!