HIF1A
From Proteopedia
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The N-terminal region of HIF1α contains a basic helix-loop-helix (bHLH) structure, that is responsible for the interaction with the hypoxia responsive elements (HRE) [5’-(G/C/T)-ACGTGC- (G/T)-3’] present in many enhancers regions of different genes, and a PERARNT-SIM (PAS) domain that are responsible for dimerization with HIF1β. HIF1β is also known as aryl hydrocarbon receptor nuclear translocator (ARNT) <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>. | The N-terminal region of HIF1α contains a basic helix-loop-helix (bHLH) structure, that is responsible for the interaction with the hypoxia responsive elements (HRE) [5’-(G/C/T)-ACGTGC- (G/T)-3’] present in many enhancers regions of different genes, and a PERARNT-SIM (PAS) domain that are responsible for dimerization with HIF1β. HIF1β is also known as aryl hydrocarbon receptor nuclear translocator (ARNT) <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 also contains a transactivation domain (TAD) that interacts with CREB binding protein (CBP) and p300, transcription co-activators. In sufficient O2 concentration <ref name="Yang">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. | HIF1α also contains a transactivation domain (TAD) that interacts with CREB binding protein (CBP) and p300, transcription co-activators. In sufficient O2 concentration <ref name="Yang">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. | ||
| - | </ref>, TAD can suffer hydroxylation by prolyl-hydroxylase (PHD) proteins, which inhibits the interaction between those co-activating factors and marks the subunit to ubiquitination by von Hippel-Lindau tumor suppressor protein (VHL), part of the E3 ubiquitin-protein ligase, and consequently degradation in the proteasome. Other interactions with different groups can inhibit the activity of HIF1α as well <ref name="Watts" | + | </ref>, TAD can suffer hydroxylation by prolyl-hydroxylase (PHD) proteins, which inhibits the interaction between those co-activating factors and marks the subunit to ubiquitination by von Hippel-Lindau tumor suppressor protein (VHL), part of the E3 ubiquitin-protein ligase, and consequently degradation in the proteasome. Other interactions with different groups can inhibit the activity of HIF1α as well <ref name="Watts"/>. |
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==References== | ==References== | ||
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Revision as of 21:36, 2 June 2024
Your Heading Here (maybe something like 'Structure')
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References
- ↑ 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.
- ↑ 2.0 2.1 .
Structure
The N-terminal region of HIF1α contains a basic helix-loop-helix (bHLH) structure, that is responsible for the interaction with the hypoxia responsive elements (HRE) [5’-(G/C/T)-ACGTGC- (G/T)-3’] present in many enhancers regions of different genes, and a PERARNT-SIM (PAS) domain that are responsible for dimerization with HIF1β. HIF1β is also known as aryl hydrocarbon receptor nuclear translocator (ARNT) <ref>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.</li> <li id="cite_note-Yang-2">[[#cite_ref-Yang_2-0|↑]] 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. </li> <li id="cite_note-Watts">[[#cite_ref-Watts_2|↑]] <strong class="error">Cite error: Invalid <code><ref></code> tag; no text was provided for refs named <code>Watts</code></strong></li> <li id="cite_note-Neil">[[#cite_ref-Neil_0|↑]] <strong class="error">Cite error: Invalid <code><ref></code> tag; no text was provided for refs named <code>Neil</code></strong></li> <li id="cite_note-Feng-5">[[#cite_ref-Feng_5-0|↑]] 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.</li>
<li id="cite_note-Cowman-6">↑ <sup>[[#cite_ref-Cowman_6-0|7.0]]</sup> <sup>[[#cite_ref-Cowman_6-1|7.1]]</sup> <sup>[[#cite_ref-Cowman_6-2|7.2]]</sup> 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.</li></ol></ref>
