In:
eLife, eLife Sciences Publications, Ltd, Vol. 5 ( 2016-01-14)
Kurzfassung:
Proteins known as hypoxia-inducible factors (HIFs) are important in animals when the amount of oxygen in the air or water drops. These proteins switch on genes that help cells and tissues adapt to the shortage in oxygen, for example, by stimulating the production of red blood cells. Each HIF is made up of two subunits called α and β that only bind to each other when the oxygen levels drop. This two-subunit complex, or 'dimer', then activates a set of genes by binding to a stretch of DNA known as the hypoxia response element. HIFs also play important roles in many different stages of animal development. There are many different HIF proteins that are each present at different developmental stages; this has made them difficult to study. Zhang et al. have found a new form of HIF-3α in zebrafish – called Hif-3α2. The experiments show that this α subunit is not regulated by oxygen, but may still be able to activate genes that have the hypoxia response element. When Hif-3α2 was injected into zebrafish embryos, the body pattern that is normally set up in embryogenesis was disrupted. Further experiments revealed that Hif-3α2 regulates embryo development by destabilizing a protein called β-catenin. This inhibits a cell communication system called Wnt/β-catenin signaling. Zhang et al. also show that the two distinct activities of Hif-3α2 – binding to the hypoxia response element and destabilizing β-catenin – involve two different regions of the protein. Together, Zhang et al.’s findings show that zebrafish Hif-3α2 combines some conventional features of HIF proteins with a unique developmental role. It is likely that human Hif-3α may also work in a similar way, so future studies will focus on understanding the molecular mechanisms responsible for these distinct roles.
Materialart:
Online-Ressource
ISSN:
2050-084X
DOI:
10.7554/eLife.08996.001
DOI:
10.7554/eLife.08996.002
DOI:
10.7554/eLife.08996.003
DOI:
10.7554/eLife.08996.004
DOI:
10.7554/eLife.08996.005
DOI:
10.7554/eLife.08996.006
DOI:
10.7554/eLife.08996.007
DOI:
10.7554/eLife.08996.008
DOI:
10.7554/eLife.08996.009
DOI:
10.7554/eLife.08996.010
DOI:
10.7554/eLife.08996.011
DOI:
10.7554/eLife.08996.012
DOI:
10.7554/eLife.08996.013
DOI:
10.7554/eLife.08996.014
DOI:
10.7554/eLife.08996.015
DOI:
10.7554/eLife.08996.016
DOI:
10.7554/eLife.08996.017
DOI:
10.7554/eLife.08996.018
DOI:
10.7554/eLife.08996.019
DOI:
10.7554/eLife.08996.020
DOI:
10.7554/eLife.08996.021
DOI:
10.7554/eLife.08996.022
DOI:
10.7554/eLife.08996.023
DOI:
10.7554/eLife.08996.024
DOI:
10.7554/eLife.08996.025
DOI:
10.7554/eLife.08996.026
DOI:
10.7554/eLife.08996.027
DOI:
10.7554/eLife.08996.028
DOI:
10.7554/eLife.08996.029
Sprache:
Englisch
Verlag:
eLife Sciences Publications, Ltd
Publikationsdatum:
2016
ZDB Id:
2687154-3