The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.

Journal article

There are three prolyl hydroxylases (PHD1, 2 and 3) that regulate the hypoxia-inducible factors (HIFs), the master transcriptional regulators that respond to changes in intracellular O(2) tension. In high O(2) tension (normoxia) the PHDs hydroxylate two conserved proline residues on HIF-1α, which leads to binding of the von Hippel-Lindau (VHL) tumour suppressor, the recognition component of a ubiquitin-ligase complex, initiating HIF-1α ubiquitylation and degradation. However, it is not known ...

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Authors: Foxler, D; Bridge, K; James, V; Webb, T; Mee, M

• Publication status: Published
• Journal: Nature cell biology
• Volume: 14
• Issue: 2
• Pages: 201-208
• Publication date: 2012-02-01
• DOI: 10.1038/ncb2424
• EISSN: 1476-4679
• ISSN: 1465-7392
• Language: English
• Keywords: Cell Hypoxia; Polyubiquitin; Hydroxylation; HEK293 Cells; Ubiquitination; Intracellular Signaling Peptides and Proteins; Immunoblotting; Two-Hybrid System Techniques; Immunoprecipitation; RNA Interference; Transfection; Humans; Protein Binding; Hela Cells; Von Hippel-Lindau Tumor Suppressor Protein; Procollagen-Proline Dioxygenase; Hypoxia-Inducible Factor 1, alpha Subunit; Cell Line, Tumor; Proteasome Endopeptidase Complex; Models, Biological; LIM Domain Proteins