Bruno Prado/Sandbox1
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
==Introduction== | ==Introduction== | ||
| - | <StructureSection load=' | + | <StructureSection load='1H2K' size='340' side='right' caption='Caption for this structure' scene=''> |
HIF1α is a subunit of the transcription factor HIF1, together with HIF1β <ref name="loboda">Loboda, Agnieszka, Alicja Jozkowicz, and Jozef Dulak. 2010. “HIF-1 and HIF-2 Transcription Factors — Similar but Not Identical.” Molecules and Cells 29 (5): 435–42. https://doi.org/10.1007/s10059-010-0067-2.</ref>. HIF1α is part exclusively of HIF1 whilst HIF1β is part of other transcription factors as well as HIF1. | HIF1α is a subunit of the transcription factor HIF1, together with HIF1β <ref name="loboda">Loboda, Agnieszka, Alicja Jozkowicz, and Jozef Dulak. 2010. “HIF-1 and HIF-2 Transcription Factors — Similar but Not Identical.” Molecules and Cells 29 (5): 435–42. https://doi.org/10.1007/s10059-010-0067-2.</ref>. HIF1α is part exclusively of HIF1 whilst HIF1β is part of other transcription factors as well as HIF1. | ||
HIF1 is related to glucose metabolism, stimulation of circulation and it was first described in hypoxia conditions, but it is now known that it can be activated also in normoxia situations, acting especially in the polarization of immune cells to more inflammatory phenotypes <ref name="oneill">O’Neill, Luke A. J., Rigel J. Kishton, and Jeff Rathmell. 2016. “A Guide to Immunometabolism for Immunologists.” Nature Reviews Immunology 16 (9): 553–65. https://doi.org/10.1038/nri.2016.70.</ref>. | HIF1 is related to glucose metabolism, stimulation of circulation and it was first described in hypoxia conditions, but it is now known that it can be activated also in normoxia situations, acting especially in the polarization of immune cells to more inflammatory phenotypes <ref name="oneill">O’Neill, Luke A. J., Rigel J. Kishton, and Jeff Rathmell. 2016. “A Guide to Immunometabolism for Immunologists.” Nature Reviews Immunology 16 (9): 553–65. https://doi.org/10.1038/nri.2016.70.</ref>. | ||
| Line 21: | Line 21: | ||
== Structural highlights == | == Structural highlights == | ||
| - | + | The HIF1α binding site to HRE is the <scene name='10/1052399/Bhlh/4'>bHLH domain</scene> (in red), this domain is responsible for the interaction between the transcription factor and the DNA, leading to the active function of HIF1α: to increase mRNA synthesis of the target genes. The <scene name='10/1052399/Nodd/1'>NODD</scene> (N-terminal oxygen dependent degradation domain), also known as N-TAD (N-terminal transactivation domain) is where the hydroxylation of HIF1α occurs, by the prolyl-hydroxylase enzymes (PHDs), targeting the transcription factor to degradation via pVHL, ubiquitination and proteasome. | |
| - | + | ||
| - | The HIF1α binding site to HRE is the <scene name='10/1052399/Bhlh/4'>bHLH domain</scene> (in red) | + | |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Introduction
| |||||||||||
References
- ↑ 1.0 1.1 Loboda, Agnieszka, Alicja Jozkowicz, and Jozef Dulak. 2010. “HIF-1 and HIF-2 Transcription Factors — Similar but Not Identical.” Molecules and Cells 29 (5): 435–42. https://doi.org/10.1007/s10059-010-0067-2.
- ↑ 2.0 2.1 2.2 O’Neill, Luke A. J., Rigel J. Kishton, and Jeff Rathmell. 2016. “A Guide to Immunometabolism for Immunologists.” Nature Reviews Immunology 16 (9): 553–65. https://doi.org/10.1038/nri.2016.70.
- ↑ YANG, Chao, Zhang-Feng ZHONG, Sheng-Peng WANG, Chi-Teng VONG, Bin YU, and Yi-Tao WANG. 2021. “HIF-1: Structure, Biology and Natural Modulators.” Chinese Journal of Natural Medicines 19 (7): 521–27. https://doi.org/10.1016/s1875-5364(21)60051-1.
- ↑ 4.0 4.1 4.2 Watts, Emily R., and Sarah R. Walmsley. 2019. “Inflammation and Hypoxia: HIF and PHD Isoform Selectivity.” Trends in Molecular Medicine 25 (1): 33–46. https://doi.org/10.1016/j.molmed.2018.10.006.
- ↑ Feng, Zhihui, Xuan Zou, Yaomin Chen, Hanzhi Wang, Yingli Duan, and Richard K Bruick. 2018. “Modulation of HIF-2α PAS-B Domain Contributes to Physiological Responses.” Proceedings of the National Academy of Sciences of the United States of America 115 (52): 13240–45. https://doi.org/10.1073/pnas.1810897115.
- ↑ 6.0 6.1 6.2 Cowman, Sophie J., and Mei Yee Koh. 2022. “Revisiting the HIF Switch in the Tumor and Its Immune Microenvironment.” Trends in Cancer 8 (1): 28–42. https://doi.org/10.1016/j.trecan.2021.10.004.
