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Mol. Cells 2010; 29(5): 435-442

Published online April 12, 2010

https://doi.org/10.1007/s10059-010-0067-2

© The Korean Society for Molecular and Cellular Biology

HIF-1 and HIF-2 Transcription Factors - Similar but Not Identical

Agnieszka Loboda*, Alicja Jozkowicz, and Jozef Dulak*

Department of Medical Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland

Correspondence to : *Correspondence: agnieszka.loboda@uj.edu.pl (AL); jozef.dulak@uj.edu.pl (JD)

Received: March 1, 2010; Accepted: March 4, 2010

Abstract

Hypoxia inducible factor (HIF)-1 and HIF-2 are heterodi-meric transcription factors mediating the cellular response to hypoxia. Recent data indicate that not only ubiquitous HIF-1α, but also more cell-specific HIF-2α, is an important regulator of the hypoxia response. Although both α subunits are highly conservative at protein level, share similar domain structure, heterodimerize with HIF-1β, and bind to the same DNA sequence called hypoxia responsive element (HRE), their effect on the expression of some genes may vary. In this review we stressed the differences between the isoforms, their structure and expression pattern. Moreover, we described diversity of coactivators and proteins which interact with HIFs, and which are responsible for the specificity of their action. Finally, recent data showing link between HIFs and specific microRNA have been presented.

Keywords c-myc, microRNA, Nrf2, prolyl hydroxylases, Ref-1

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Mol. Cells 2010; 29(5): 435-442

Published online May 31, 2010 https://doi.org/10.1007/s10059-010-0067-2

Copyright © The Korean Society for Molecular and Cellular Biology.

HIF-1 and HIF-2 Transcription Factors - Similar but Not Identical

Agnieszka Loboda*, Alicja Jozkowicz, and Jozef Dulak*

Department of Medical Biotechnology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland

Correspondence to:*Correspondence: agnieszka.loboda@uj.edu.pl (AL); jozef.dulak@uj.edu.pl (JD)

Received: March 1, 2010; Accepted: March 4, 2010

Abstract

Hypoxia inducible factor (HIF)-1 and HIF-2 are heterodi-meric transcription factors mediating the cellular response to hypoxia. Recent data indicate that not only ubiquitous HIF-1α, but also more cell-specific HIF-2α, is an important regulator of the hypoxia response. Although both α subunits are highly conservative at protein level, share similar domain structure, heterodimerize with HIF-1β, and bind to the same DNA sequence called hypoxia responsive element (HRE), their effect on the expression of some genes may vary. In this review we stressed the differences between the isoforms, their structure and expression pattern. Moreover, we described diversity of coactivators and proteins which interact with HIFs, and which are responsible for the specificity of their action. Finally, recent data showing link between HIFs and specific microRNA have been presented.

Keywords: c-myc, microRNA, Nrf2, prolyl hydroxylases, Ref-1

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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