Cited by 25Retinoids in leukemia and cellular processesUbiquitin and proteasome pathwaysGenomics and Chromatin Dynamics

SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3

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Ferry, Christine, Gianni, Maurizio, Lalevée, Sébastien, Bruck, Nathalie, Plassat, Jean-Luc, Raska, Ivan, Garattini, Enrico, Rochette-Egly, Cécile·2009·Journal of Biological Chemistry

Abstract

Nuclear retinoic acid receptor alpha (RARalpha) 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 RARalpha. Then RARalpha and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARalpha-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 RARalpha target genes and the degradation of RARalpha 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 RARalpha. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARalpha 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.

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Crossref · 10.1074/jbc.m808815200

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  • RARs are also degraded by the ubiquitin-proteasome system, through the recruitment of TRIP1/SUG-1, which is a subunit of the 19S regulatory subcomplex of the proteasome with an ATPase activity.

    “RARs are also degraded by the ubiquitin-proteasome system, through the recruitment of TRIP1/SUG-1, which is a subunit of the 19S regulatory subcomplex of the proteasome with an ATPase activity ( 110-112 ).”

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Authors
Ferry, C., Gianni, M., Lalevée, S., Bruck, N., Plassat, J.-L., Raska, I., Garattini, E., & Rochette-Egly, C.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Mario Negri Institute for Pharmacological Research (IT)
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2009-03
Volume
284
Issue
12
Pages
8127-8135
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2087685666
Cited by
24
References
47
Citations by year
2024: 1 · 2023: 1 · 2022: 4 · 2021: 1 · 2017: 1 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 3
FWCI
1.21
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Funders
Agence Nationale de la Recherche (ANR-05-BLAN-0390)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
SRC-3, retinoic acid receptor alpha, 19S proteasome, proteasomal degradation, transcriptional regulation, coregulator recruitment, AF-2 domain, 26S proteasome, protein-protein interaction, gene expression
MeSH terms
Retinoic Acid Receptor alpha, ATPases Associated with Diverse Cellular Activities, Animals, Chlorocebus aethiops, Gene Expression Regulation, HeLa Cells, Humans, Models, Biological, Transcription Factors, Transcription, Genetic, Tretinoin, Trans-Activators, Protein Structure, Tertiary, Receptors, Retinoic Acid, COS Cells, Proteasome Endopeptidase Complex, Adaptor Proteins, Signal Transducing, Histone Acetyltransferases, Nuclear Receptor Coactivator 3, LIM Domain Proteins

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