Article

Erythrocytosis-inducing PHD2 mutations implicate biological role for N-terminal prolyl-hydroxylation in HIF1α oxygen-dependent degradation domain

2025-04-24

Abstract excerpt

<h4>ABSTRACT</h4> Mutations in EGLN1 , the gene encoding for hypoxia-inducible factor (HIF) prolyl-4-hydroxylase 2 (PHD2), cause erythrocytosis and in rare cases the development of neuroendocrine tumors. In the presence of oxygen, PHD2 hydroxylates one or both conserved prolines in the oxygen-dependent degradation domain (ODD) of HIFα subunits, sufficiently marking HIFα for binding and ubiquitylation via the von...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: d584817f-07d4-5d4d-b933-4ae7fe13bf62
DOI: 10.1101/2025.04.22.650142

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Erythrocytosis-inducing PHD2 mutations implicate biological role for N-terminal prolyl-hydroxylation in HIF1α oxygen-dependent degradation domainDOI 10.1101/2025.04.22.650142Read

The role of PHD2 mutations in the pathogenesis of erythrocytosisSemantic proximity Read

Novel <i>EGLN1</i> variants identified in patients with erythrocytosis: a functional studySemantic proximity Read

Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline.Semantic proximity Read

Isolated erythrocytosis: study of 67 patients and identification of three novel germ-line mutations in the prolyl hydroxylase domain protein 2 (PHD2) geneSemantic proximity Read

Characterization of genetic variants in the EGLN1/PHD2 gene identified in a European collection of patients with erythrocytosisSemantic proximity Read

A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove.Semantic proximity Read

Biochemical characterization of human prolyl hydroxylase domain protein 2 variants associated with erythrocytosis.Semantic proximity Read

Sequence determinants in hypoxia-inducible factor-1alpha for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3.Semantic proximity Read

Cardiopulmonary phenotype associated with human PHD2 mutation.Semantic proximity Read

Leu-574 of human HIF-1alpha is a molecular determinant of prolyl hydroxylation.Semantic proximity Read

Inactivation of HIF-P4H-1 Stabilizes IKKα, Modulates Non-Canonical NF-κB Signaling, and Sensitizes Cancer Cells to Cell DeathSemantic proximity Read

Coordinate regulation of the oxygen-dependent degradation domains of hypoxia-inducible factor 1 alpha.Semantic proximity Read