Cited by 232Cancer, Hypoxia, and MetabolismUbiquitin and proteasome pathwaysKruppel-like factors research

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Sumoylation increases HIF-1α stability and its transcriptional activity

Bae, Seong-Hui, Jeong, Joo-Won, Park, Jeong Ae, Kim, Se-Hee, Bae, Moon-Kyoung, Choi, Soo-Joon, Kim, Kyu-Won·2004·Biochemical and Biophysical Research Communications

DOI 10.1016/j.bbrc.2004.09.068

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Abstract

HIF-1 is closely involved in various biological processes, including angiogenesis, energy metabolism, and cell survival. HIF-1 consists of an oxygen-sensitive HIF-1alpha and oxygen-insensitive HIF-1beta. Oxygen-sensitive HIF-1alpha is subjected to post-translational modifications such as hydroxylation, ubiquitination, and acetylation, which are related to the regulation of its stability. In this present study, we found that the ectopic expression of SUMO-1 increased HIF-1alpha stability by the co-transfection study with HIF-1alpha and SUMO-1. Furthermore, the ectopic expression of SUMO-1 enhanced the transcriptional activity of HIF-1alpha. In the subsequent immunoprecipitation assay, SUMO-1 was co-immunoprecipitated with HIF-1alpha, implying that HIF-1alpha is covalently modified by SUMO-1. Thereafter, using a series of lysine mutants in the ODD domain, we found that HIF-1alpha was sumoylated at Lys(391) and Lys(477), suggesting that sumoylation at these two lysine residues enhances HIF-1alpha stability by possibly modulating other post-translational modifications. Altogether, we demonstrate that HIF-1alpha is upregulated through SUMO-1 modification at Lys(391)/Lys(477) residues, which may stabilize HIF-1alpha and enhance its transcriptional activity.

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Authors: Bae, S.-H., Jeong, J.-W., Park, J. A., Kim, S.-H., Bae, M.-K., Choi, S.-J., & Kim, K.-W.
Affiliations: Seoul National University (KR)
Harvard University (US)
Pusan National University (KR)
Corresponding author: Kim, Kyu-Won
ORCID: Jeong, Joo-Won
Bae, Moon-Kyoung
Kim, Kyu-Won
Venue: Biochemical and Biophysical Research Communications
Publisher: Elsevier BV
Published: 2004-11
Volume: 324
Issue: 1
Pages: 394-400
ISSN: 0006-291X (ISSN-L)
DOI: 10.1016/j.bbrc.2004.09.068
OpenAlex: W2085483520
Cited by: 232
References: 26
Citations by year: 2026: 5 · 2025: 10 · 2024: 15 · 2023: 8 · 2022: 12 · 2021: 8 · 2020: 7 · 2019: 5 · 2018: 8 · 2017: 8 · 2016: 9 · 2015: 11 · 2014: 16 · 2013: 12 · 2012: 8
FWCI: 3.72
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochemical and Biophysical Research Communications (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Kruppel-like factors research
Keywords: HIF-1α, SUMOylation, SUMO1, protein stability, transcriptional activity, lysine modification, post-translational modification, ARNT, oxygen sensing, lysine mutants
MeSH terms: Amino Acid Sequence, Animals, Enzyme Stability, HeLa Cells, Humans, Lysine, Molecular Sequence Data, Protein Processing, Post-Translational, Transcription Factors, Transcription, Genetic, Gene Expression Regulation, Enzymologic, SUMO-1 Protein, Hypoxia-Inducible Factor 1, alpha Subunit

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Sumoylation increases HIF-1α stability and its transcriptional activity

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