HIF1A: Difference between revisions
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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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