Cargando…

Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity

Over the past few years, small ubiquitin-like modifier (SUMO) modification has emerged as an important regulator of diverse pathways and activities including protein localization and transcriptional regulation. We identified a consensus sumoylation motif (IKEE), located within the N-terminal activat...

Descripción completa

Detalles Bibliográficos
Autores principales: Hamard, Pierre-Jacques, Boyer-Guittaut, Michaël, Camuzeaux, Barbara, Dujardin, Denis, Hauss, Charlotte, Oelgeschläger, Thomas, Vigneron, Marc, Kedinger, Claude, Chatton, Bruno
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1851647/
https://www.ncbi.nlm.nih.gov/pubmed/17264123
http://dx.doi.org/10.1093/nar/gkl1168
_version_ 1782132975809331200
author Hamard, Pierre-Jacques
Boyer-Guittaut, Michaël
Camuzeaux, Barbara
Dujardin, Denis
Hauss, Charlotte
Oelgeschläger, Thomas
Vigneron, Marc
Kedinger, Claude
Chatton, Bruno
author_facet Hamard, Pierre-Jacques
Boyer-Guittaut, Michaël
Camuzeaux, Barbara
Dujardin, Denis
Hauss, Charlotte
Oelgeschläger, Thomas
Vigneron, Marc
Kedinger, Claude
Chatton, Bruno
author_sort Hamard, Pierre-Jacques
collection PubMed
description Over the past few years, small ubiquitin-like modifier (SUMO) modification has emerged as an important regulator of diverse pathways and activities including protein localization and transcriptional regulation. We identified a consensus sumoylation motif (IKEE), located within the N-terminal activation domain of the ATF7 transcription factor and thus investigated the role of this modification. ATF7 is a ubiquitously expressed transcription factor, homologous to ATF2, that binds to CRE elements within specific promoters. This protein is able to heterodimerize with Jun or Fos proteins and its transcriptional activity is mediated by interaction with TAF12, a subunit of the general transcription factor TFIID. In the present article, we demonstrate that ATF7 is sumoylated in vitro (using RanBP2 as a E3-specific ligase) and in vivo. Moreover, we show that ATF7 sumoylation affects its intranuclear localization by delaying its entry into the nucleus. Furthermore, SUMO conjugation inhibits ATF7 transactivation activity by (i) impairing its association with TAF12 and (ii) blocking its binding-to-specific sequences within target promoters.
format Text
id pubmed-1851647
institution National Center for Biotechnology Information
language English
publishDate 2007
publisher Oxford University Press
record_format MEDLINE/PubMed
spelling pubmed-18516472007-04-26 Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity Hamard, Pierre-Jacques Boyer-Guittaut, Michaël Camuzeaux, Barbara Dujardin, Denis Hauss, Charlotte Oelgeschläger, Thomas Vigneron, Marc Kedinger, Claude Chatton, Bruno Nucleic Acids Res Molecular Biology Over the past few years, small ubiquitin-like modifier (SUMO) modification has emerged as an important regulator of diverse pathways and activities including protein localization and transcriptional regulation. We identified a consensus sumoylation motif (IKEE), located within the N-terminal activation domain of the ATF7 transcription factor and thus investigated the role of this modification. ATF7 is a ubiquitously expressed transcription factor, homologous to ATF2, that binds to CRE elements within specific promoters. This protein is able to heterodimerize with Jun or Fos proteins and its transcriptional activity is mediated by interaction with TAF12, a subunit of the general transcription factor TFIID. In the present article, we demonstrate that ATF7 is sumoylated in vitro (using RanBP2 as a E3-specific ligase) and in vivo. Moreover, we show that ATF7 sumoylation affects its intranuclear localization by delaying its entry into the nucleus. Furthermore, SUMO conjugation inhibits ATF7 transactivation activity by (i) impairing its association with TAF12 and (ii) blocking its binding-to-specific sequences within target promoters. Oxford University Press 2007-02 2007-01-30 /pmc/articles/PMC1851647/ /pubmed/17264123 http://dx.doi.org/10.1093/nar/gkl1168 Text en © 2007 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Molecular Biology
Hamard, Pierre-Jacques
Boyer-Guittaut, Michaël
Camuzeaux, Barbara
Dujardin, Denis
Hauss, Charlotte
Oelgeschläger, Thomas
Vigneron, Marc
Kedinger, Claude
Chatton, Bruno
Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title_full Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title_fullStr Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title_full_unstemmed Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title_short Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
title_sort sumoylation delays the atf7 transcription factor subcellular localization and inhibits its transcriptional activity
topic Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1851647/
https://www.ncbi.nlm.nih.gov/pubmed/17264123
http://dx.doi.org/10.1093/nar/gkl1168
work_keys_str_mv AT hamardpierrejacques sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT boyerguittautmichael sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT camuzeauxbarbara sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT dujardindenis sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT hausscharlotte sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT oelgeschlagerthomas sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT vigneronmarc sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT kedingerclaude sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity
AT chattonbruno sumoylationdelaystheatf7transcriptionfactorsubcellularlocalizationandinhibitsitstranscriptionalactivity