SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3

Christine Ferry, Maurizio Gianni, Sébastien Lalevée, Nathalie Bruck, Jean Luc Plassat, Ivan Raska, Enrico Garattini, Cécile Rochette-Egly

Research output: Contribution to journalArticle

Abstract

Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARa. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.

Original languageEnglish
Pages (from-to)8127-8135
Number of pages9
JournalJournal of Biological Chemistry
Volume284
Issue number12
DOIs
Publication statusPublished - Mar 20 2009

Fingerprint

Retinoic Acid Receptors
Tretinoin
Genes
Transcription
Furylfuramide
Proteasome Endopeptidase Complex
Degradation
Gene expression
Adenosine Triphosphatases
Chemical activation
Ligands
Gene Expression

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3. / Ferry, Christine; Gianni, Maurizio; Lalevée, Sébastien; Bruck, Nathalie; Plassat, Jean Luc; Raska, Ivan; Garattini, Enrico; Rochette-Egly, Cécile.

In: Journal of Biological Chemistry, Vol. 284, No. 12, 20.03.2009, p. 8127-8135.

Research output: Contribution to journalArticle

Ferry, Christine ; Gianni, Maurizio ; Lalevée, Sébastien ; Bruck, Nathalie ; Plassat, Jean Luc ; Raska, Ivan ; Garattini, Enrico ; Rochette-Egly, Cécile. / SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3. In: Journal of Biological Chemistry. 2009 ; Vol. 284, No. 12. pp. 8127-8135.
@article{80e98991e0154b34b4b5ec291294903b,
title = "SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3",
abstract = "Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARa. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.",
author = "Christine Ferry and Maurizio Gianni and S{\'e}bastien Lalev{\'e}e and Nathalie Bruck and Plassat, {Jean Luc} and Ivan Raska and Enrico Garattini and C{\'e}cile Rochette-Egly",
year = "2009",
month = "3",
day = "20",
doi = "10.1074/jbc.M808815200",
language = "English",
volume = "284",
pages = "8127--8135",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "12",

}

TY - JOUR

T1 - SUG-1 plays proteolytic and non-proteolytic roles in the control of retinoic acid target genes via its interaction with SRC-3

AU - Ferry, Christine

AU - Gianni, Maurizio

AU - Lalevée, Sébastien

AU - Bruck, Nathalie

AU - Plassat, Jean Luc

AU - Raska, Ivan

AU - Garattini, Enrico

AU - Rochette-Egly, Cécile

PY - 2009/3/20

Y1 - 2009/3/20

N2 - Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARa. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.

AB - Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARa. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.

UR - http://www.scopus.com/inward/record.url?scp=65549158253&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=65549158253&partnerID=8YFLogxK

U2 - 10.1074/jbc.M808815200

DO - 10.1074/jbc.M808815200

M3 - Article

C2 - 19144644

AN - SCOPUS:65549158253

VL - 284

SP - 8127

EP - 8135

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 12

ER -