Document Detail


Mutual regulation of c-Jun and ATF2 by transcriptional activation and subcellular localization.
MedLine Citation:
PMID:  16511568     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
ATF2 and c-Jun are key components of activating protein-1 and function as homodimers or heterodimers. c-Jun-ATF2 heterodimers activate the expression of many target genes, including c-jun, in response to a variety of cellular and environmental signals. Although it has been believed that c-Jun and ATF2 are constitutively localized in the nucleus, where they are phosphorylated and activated by mitogen-activated protein kinases, the molecular mechanisms underlying the regulation of their transcriptional activities remain to be defined. Here we show that ATF2 possesses a nuclear export signal in its leucine zipper region and two nuclear localization signals in its basic region, resulting in continuous shuttling between the cytoplasm and the nucleus. Dimerization with c-Jun in the nucleus prevents the export of ATF2 and is essential for the transcriptional activation of the c-jun promoter. Importantly, c-Jun-dependent nuclear localization of ATF2 occurs during retinoic acid-induced differentiation and UV-induced cell death in F9 cells. Together, these findings demonstrate that ATF2 and c-Jun mutually regulate each other by altering the dynamics of subcellular localization and by positively impacting transcriptional activity.
Authors:
Han Liu; Xuehong Deng; Y John Shyu; Jian Jian Li; Elizabeth J Taparowsky; Chang-Deng Hu
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2006-03-02
Journal Detail:
Title:  The EMBO journal     Volume:  25     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-03-08     Completed Date:  2006-04-17     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  1058-69     Citation Subset:  IM    
Affiliation:
Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
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MeSH Terms
Descriptor/Qualifier:
Activating Transcription Factor 2 / genetics,  metabolism*
Amino Acid Sequence
Animals
Antineoplastic Agents / pharmacology
COS Cells
Cell Differentiation / drug effects
Cell Nucleus / metabolism
Cercopithecus aethiops
Cytoplasm / metabolism
Gene Expression Regulation*
Humans
Molecular Sequence Data
Mutation / genetics
Promoter Regions, Genetic / genetics
Protein Transport
Proto-Oncogene Proteins c-jun / genetics,  metabolism*
Sequence Homology, Amino Acid
Transcription Factor AP-1 / genetics,  metabolism
Transcription, Genetic
Transcriptional Activation*
Tretinoin / pharmacology
Ultraviolet Rays
Grant Support
ID/Acronym/Agency:
CA101990/CA/NCI NIH HHS; CA78264/CA/NCI NIH HHS; P30CA23168/CA/NCI NIH HHS; R01 CA101990/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/ATF2 protein, human; 0/Activating Transcription Factor 2; 0/Antineoplastic Agents; 0/Proto-Oncogene Proteins c-jun; 0/Transcription Factor AP-1; 302-79-4/Tretinoin
Comments/Corrections
Erratum In:
EMBO J. 2006 Jun 21;25(12):2952

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


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