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

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Poukka, Hetti, Karvonen, Ulla, Jänne, Olli A., Palvimo, Jorma J.·2000·Proceedings of the National Academy of Sciences

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.

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Metadata

Authors
Poukka, H., Karvonen, U., Jänne, O. A., & Palvimo, J. J.
Venue
Proceedings of the National Academy of Sciences
Published
2000-12-19
Volume
97
Issue
26
Pages
14145-14150
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975658312
Cited by
457
References
0
FWCI
25.47
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). https://app.cochat.ai/papers/10.1073/pnas.97.26.14145
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Poukka, H., Karvonen, U., Jänne, O. A., & Palvimo, J. J. (2000). Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.26.14145

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.