Insights into The Function and Regulation of Jumonji C Lysine Demethylases as Hypoxic Responsive Enzymes.

Insights into The Function and Regulation of Jumonji C Lysine Demethylases as Hypoxic Responsive Enzymes.
Curr Protein Pept Sci. 2019 Dec 30;:
Authors: Chopra A, Adhikary H, Willmore WG, Biggar KK
Abstract
Cellular responses to hypoxia (low oxygen) are governed by oxygen sensitive signalling pathways. Such pathways, in part, are controlled by enzymes with oxygen-dependent catalytic activity, of which the role of prolyl 4-hydroxylases has been widely reviewed. These enzymes inhibit hypoxic response by inducing the oxygen-dependent degradation of hypoxia-inducible factor 1α, the master regulator of transcriptional hypoxic response. Jumonji C domain-containing lysine demethylases are similar enzymes which share the same oxygen-dependent catalytic mechanism as prolyl 4-hydroxylases. Traditionally, the role of lysine demethylases has been studied in relation to demethylation activity against histone substrates, however, within the past decade an increasing number of non-histone protein targets have been revealed, some of which have a key role in survival in the hypoxic tumor microenvironment. Within this review we highlight the involvement of methyllysine in the hypoxic response with a focus on the HIF signalling pathway, the regulation of demethylase activity by oxygen, and provide insights into notable areas of future hypoxic demethylase research.
PMID: 31889485 [PubMed - as supplied by publisher]

Source: Current Protein and Peptide Science - December 29, 2019 Category: Biochemistry Authors: Chopra A, Adhikary H, Willmore WG, Biggar KK Tags: Curr Protein Pept Sci Source Type: research