| http://purl.uniprot.org/citations/20811646 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20811646 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundThe Hypoxia Inducible Factor (HIF) mediates cellular adaptations to low oxygen. Prolyl-4-hydroxylases are oxygen sensors that hydroxylate the HIF alpha-subunit, promoting its proteasomal degradation in normoxia. Three HIF-prolyl hydroxylases, encoded by independent genes, PHD1, PHD2, and PHD3, occur in mammals. PHD2, the longest PHD isoform includes a MYND domain, whose biochemical function is unclear. PHD2 and PHD3 genes are induced in hypoxia to shut down HIF dependent transcription upon reoxygenation, while expression of PHD1 is oxygen-independent. The physiologic significance of the diversity of the PHD oxygen sensors is intriguing.Methodology and principal findingsWe have analyzed the Drosophila PHD locus, fatiga, which encodes 3 isoforms, FgaA, FgaB and FgaC that are originated through a combination of alternative initiation of transcription and alternative splicing. FgaA includes a MYND domain and is homologous to PHD2, while FgaB and FgaC are shorter isoforms most similar to PHD3. Through a combination of genetic experiments in vivo and molecular analyses in cell culture, we show that fgaB but not fgaA is induced in hypoxia, in a Sima-dependent manner, through a HIF-Responsive Element localized in the first intron of fgaA. The regulatory capacity of FgaB is stronger than that of FgaA, as complete reversion of fga loss-of-function phenotypes is observed upon transgenic expression of the former, and only partial rescue occurs after expression of the latter.Conclusions and significanceDiversity of PHD isoforms is a conserved feature in evolution. As in mammals, there are hypoxia-inducible and non-inducible Drosophila PHDs, and a fly isoform including a MYND domain co-exists with isoforms lacking this domain. Our results suggest that the isoform devoid of a MYND domain has stronger regulatory capacity than that including this domain."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0012390"xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/author | "Wappner P."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/author | "Acevedo J.M."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/author | "Centanin L."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/author | "Dekanty A."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/pages | "e12390"xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/title | "Oxygen sensing in Drosophila: multiple isoforms of the prolyl hydroxylase fatiga have different capacity to regulate HIFalpha/Sima."xsd:string |
| http://purl.uniprot.org/citations/20811646 | http://purl.uniprot.org/core/volume | "5"xsd:string |
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