The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Redox-Regulated Recruitment of the Transcriptional Coactivators CREB-Binding Protein and SRC-1 to Hypoxia-Inducible Factor 1α
Open accessAbstract
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.
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Cites
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Self-citationE1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
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“CBP and p300 are closely related proteins that exhibit strong sequence similarity and similar functions with respect to their roles as coactivators (3, 4, 11, 36).”
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Cited by
Hypoxia — a key regulatory factor in tumour growth
Harris, A. L. (2002) · Nature Reviews Cancer · doi:10.1038/nrc704 · Cited by 5,177
Hypoxia-Inducible Factor-1 (HIF-1)
Ke, Q., & Costa, M. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.027029 · Cited by 1,646
Asparagine Hydroxylation of the HIF Transactivation Domain: A Hypoxic Switch
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Differential Roles of Hypoxia-Inducible Factor 1α (HIF-1α) and HIF-2α in Hypoxic Gene Regulation
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Metadata
- Authors
- Carrero, P., Okamoto, K., Coumailleau, P., O'Brien, S., Tanaka, H., & Poellinger, L.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-01
- Volume
- 20
- Issue
- 1
- Pages
- 402-415
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2155415917
- Cited by
- 385
- References
- 8
- FWCI
- 13.12
- Type
- journal article
- Language
- en
- Open access
- green
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- Carrero, P., Okamoto, K., Coumailleau, P., O'Brien, S., Tanaka, H., & Poellinger, L. (2000). Redox-Regulated Recruitment of the Transcriptional Coactivators CREB-Binding Protein and SRC-1 to Hypoxia-Inducible Factor 1α. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.20.1.402-415.2000
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