Document Detail

RE-1 silencing transcription factor (REST) regulates human synaptophysin gene transcription through an intronic sequence-specific DNA-binding site.
MedLine Citation:
PMID:  12492469     Owner:  NLM     Status:  MEDLINE    
Synaptophysin, one of the major proteins on synaptic vesicles, is ubiquitously expressed throughout the brain. Synaptophysin and synapsin I, another synaptic vesicle protein, are also expressed by retinoic acid-induced neuronally differentiated P19 teratocarcinoma cells. Here, we show that inhibition of histone deacetylase activity in P19 cells is sufficient to activate transcription of the synaptophysin and synapsin I genes, indicating that neuronal differentiation and impairment of histone deacetylases results in a similar gene expression pattern. The transcription factor REST, a repressor of neuronal genes in non-neuronal tissues, has been shown to function via recruitment of histone deacetylases to the transcription unit, indicating that modulation of the chromatin structure via histone deacetylation is of major importance for REST function and neuron-specific gene transcription. Furthermore, REST has been shown to be the major regulator of neuronal expression of synapsin I. Here, we have identified a functional binding site for REST in the first intron of the human synaptophysin gene indicating that REST blocks human synaptophysin gene transcription through an intronic neuron-specific silencer element. The synaptophysin promoter is, however, devoid of neuron-specific genetic elements and directs transcription in both neuronal and non-neuronal cells. Using a dominant-negative approach we have identified the transcription factor Sp1 as one of the regulators responsible for constitutive transcription of the human synaptophysin gene.
Michael Lietz; Mathias Hohl; Gerald Thiel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  270     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  2003 Jan 
Date Detail:
Created Date:  2002-12-20     Completed Date:  2003-02-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  2-9     Citation Subset:  IM    
Department of Medical Biochemistry and Molecular Biology, University of Saarland Medical Center, Homburg, Germany.
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MeSH Terms
Amino Acid Sequence
Binding Sites
Cells, Cultured
DNA-Binding Proteins / genetics,  metabolism
Enzyme Inhibitors / pharmacology
Gene Expression Regulation
Hydroxamic Acids / pharmacology
Molecular Sequence Data
Neurons / physiology
Promoter Regions, Genetic
Repressor Proteins / genetics,  metabolism*
Sp1 Transcription Factor / genetics,  metabolism
Synapsins / genetics,  metabolism
Synaptophysin / genetics*,  metabolism*
Teratocarcinoma / genetics,  pathology
Testicular Neoplasms / genetics,  pathology
Transcription Factors / genetics,  metabolism*
Transcription, Genetic / drug effects
Tretinoin / pharmacology
Reg. No./Substance:
0/DNA-Binding Proteins; 0/Enzyme Inhibitors; 0/Hydroxamic Acids; 0/RE1-silencing transcription factor; 0/Repressor Proteins; 0/Sp1 Transcription Factor; 0/Synapsins; 0/Synaptophysin; 0/Transcription Factors; 302-79-4/Tretinoin; 58880-19-6/trichostatin A

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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