Oxygen-dependent hydroxylation of critical proline residues, catalyzed by prolyl hydroxylase (PHD1-3) enzymes, is a crucial posttranslational modification (PTM) within the canonical hypoxia-inducible factor (HIF)-centric cellular oxygen-sensing pathway. Alteration of substrates in this way often leads to protea-somal degradation mediated by the von Hippel-Lindau Tumor Suppressor protein (VHL) containing E3-ubiquitin ligase complex known as ECV (Elongins B/C, CUL2, VHL). Here, we outline in vitro protocols to demonstrate the ability of VHL to bind to a prolyl-hydroxylated substrate.
CITATION STYLE
Heir, P., & Ohh, M. (2016). Hydroxylation-dependent interaction of substrates to the von hippel-lindau tumor suppressor protein (VHL). In Methods in Molecular Biology (Vol. 1458, pp. 87–94). Humana Press Inc. https://doi.org/10.1007/978-1-4939-3801-8_7
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