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Molecular and Cellular Biology, January 2000, p. 402-415, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Redox-Regulated Recruitment of the Transcriptional Coactivators CREB-Binding Protein and SRC-1 to Hypoxia-Inducible Factor 1alpha

Pilar Carrero,1 Kensaku Okamoto,1,2 Pascal Coumailleau,1,dagger Sallyann O'Brien,1 Hirotoshi Tanaka,3 and Lorenz Poellinger1,*

Department of Cell and Molecular Biology, Karolinska Institutet, S-171 77 Stockholm, Sweden,1 and Second Department of Internal Medicine, Asahikawa Medical College, Asahikawa 078-8510,2 and Department of Clinical Immunology and AIDS Research Center Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639,3 Japan

Received 29 March 1999/Returned for modification 20 May 1999/Accepted 14 September 1999

Hypoxia-inducible factor 1alpha (HIF-1alpha ) functions as a transcription factor that is activated by decreased cellular oxygen concentrations to induce expression of a network of genes involved in angiogenesis, erythropoiesis, and glucose homeostasis. Here we demonstrate that two members of the SRC-1/p160 family of transcriptional coactivators harboring histone acetyltransferase activity, SRC-1 and transcription intermediary factor 2 (TIF2), are able to interact with HIF-1alpha and enhance its transactivation potential in a hypoxia-dependent manner. HIF-1alpha contains within its C terminus two transactivation domains. The hypoxia-inducible activity of both these domains was enhanced by either SRC-1 or the CREB-binding protein (CBP)/p300 coactivator. Moreover, at limiting concentrations, SRC-1 produced this effect in synergy with CBP. Interestingly, this effect was strongly potentiated by the redox regulatory protein Ref-1, a dual-function protein harboring DNA repair endonuclease and cysteine reducing activities. These data indicate that all three proteins, CBP, SRC-1, and Ref-1, are important components of the hypoxia signaling pathway and have a common function in regulation of HIF-1alpha function in hypoxic cells. Given the absence of cysteine residues in one of the Ref-1-regulated transactivation domains of HIF-1alpha , it is thus possible that Ref-1 functions in hypoxic cells by targeting critical steps in the recruitment of the CBP-SRC-1 coactivator complex.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology, Karolinska Institutet, S-171 77 Stockholm, Sweden. Phone: 46-8 728 7330. Fax: 46-8 34 88 19. E-mail: Lorenz.Poellinger{at}cmb.ki.se.

dagger Present address: Department of Molecular and Cellular Biology of Development, Genes and Development Laboratory, UMR CNRS 7622, Universite Pierre et Marie Curie, 75252 Paris Cedex 05, France.

Molecular and Cellular Biology, January 2000, p. 402-415, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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