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PMID: 11121022 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1).

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 97 ·No. 26 ·2000-12-19 ·Pages 14145-50

Poukka H, Karvonen U, Janne OA, Palvimo JJ

Abstract

Modification by SUMO-1 is proposed to play a role in protein targeting and/or stability. The SUMO-1-conjugating enzyme Ubc9 interacts with androgen receptor (AR), a ligand-activated transcription factor belonging to the steroid receptor superfamily. We show here that AR is covalently modified by SUMO-1 (sumoylated) in an androgen-enhanced fashion and identify the principal acceptor site in the N-terminal domain of AR. Substitutions of sumoylated Lys residues enhanced transcriptional activity of AR without influencing its transrepressing activity. Interestingly, the same Lys residues form the cores of the recently described transcriptional synergy control motifs in AR [Iñiguez-Lluhi, J. A. & Pearce, D. (2000) Mol. Cell. Biol. 20, 6040-6050]. These motifs, which match perfectly with the sumoylation consensus sequence, are also present in the N-terminal domains of glucocorticoid, mineralocorticoid, and progesterone receptor. Taken together, our data suggest that reversible sumoylation is a mechanism for regulation of steroid receptor function.

MeSH Terms
Animals Binding Sites COS Cells Catalysis Chlorocebus aethiops HeLa Cells Humans Ligases/metabolism Receptors, Androgen/genetics,metabolism Recombinant Fusion Proteins/genetics,metabolism SUMO-1 Protein Transcription, Genetic Ubiquitin-Conjugating Enzymes Ubiquitins/genetics,metabolism
Chemicals
Receptors, Androgen Recombinant Fusion Proteins SUMO-1 Protein Ubiquitins Ubiquitin-Conjugating Enzymes Ligases ubiquitin-conjugating enzyme UBC9
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Poukka H
Department of Physiology, Institute of Biomedicine, and Department of Clinical Chemistry, University of Helsinki, FIN-00014, Helsinki, Finland.
Karvonen U
Janne O A
Palvimo J J
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.97.26.14145
Published
2000-12-19
Pages
14145-50
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC18885
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.97.26.14145 PMC Full Text View journal details
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