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- W2001666774 abstract "Oxygen-sensing prolyl hydroxylase domain enzymes (PHDs) target hypoxia-inducible factor (HIF)-α subunits for proteasomal degradation in normoxia through hydroxylation. Recently, novel mechanisms of PHD activation and function have been unveiled. Interestingly, PHD3 can unexpectedly amplify HIF signaling through hydroxylation of the glycolytic enzyme pyruvate kinase (PK) muscle isoform 2 (PKM2). Recent studies have also yielded insight into HIF-independent PHD functions, including the control of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor trafficking in synaptic transmission and the activation of transient receptor potential cation channel member A1 (TRPA1) ion channels by oxygen levels in sensory nerves. Finally, PHD activation has been shown to involve the iron chaperoning function of poly(rC) binding protein (PCBP)1 and the (R)-enantiomer of 2-hydroxyglutarate (2-HG). The intersection of these regulatory pathways and interactions highlight the complexity of PHD regulation and function." @default.
- W2001666774 created "2016-06-24" @default.
- W2001666774 creator A5006056577 @default.
- W2001666774 creator A5047152113 @default.
- W2001666774 creator A5057422837 @default.
- W2001666774 creator A5059055814 @default.
- W2001666774 date "2013-01-01" @default.
- W2001666774 modified "2023-10-02" @default.
- W2001666774 title "Emerging novel functions of the oxygen-sensing prolyl hydroxylase domain enzymes" @default.
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