TY - JOUR
T1 - Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
AU - Hamard, Pierre Jacques
AU - Boyer-Guittaut, Michaël
AU - Camuzeaux, Barbara
AU - Dujardin, Denis
AU - Hauss, Charlotte
AU - Oelgeschläger, Thomas
AU - Vigneron, Marc
AU - Kedinger, Claude
AU - Chatton, Bruno
N1 - Funding Information:
We thank P. O’Hare, D. Bailey, V. Doye, J.L. Bocco, B. Wasylyk, A. Werner, J. Seeler, M.Donzeau and J. De Mey for gifts and helpful discussions. This work was supported by funds and/or fellowships from the Centre National de la Recherche Scientifique, the Université Louis Pasteur de Strasbourg, the French Ministry of Research, the Institut National de la Santé et de la Recherche Médicale, the Association pour la Recherche sur le Cancer (contract 3712) and the Ligue Nationale contre le Cancer—Comités Alsace (Haut-Rhin et Bas-Rhin) et Vosges. Funding to pay the Open Access publication charge was provided by the Association pour la Recherche sur le Cancer.
PY - 2007/2
Y1 - 2007/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34047127403&partnerID=8YFLogxK
U2 - 10.1093/nar/gkl1168
DO - 10.1093/nar/gkl1168
M3 - Article
C2 - 17264123
AN - SCOPUS:34047127403
SN - 0305-1048
VL - 35
SP - 1134
EP - 1144
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 4
ER -