pVHL mediates K63-linked ubiquitination of nCLU

• Published in: PloS one Vol. 7; no. 4; p. e35848
• Main Authors: Xue, Jing, Lv, Dan-Dan, Jiao, Shi, Zhao, Wenting, Li, Xuebing, Sun, Heng, Yan, Bing, Fan, Li, Hu, Rong-Gui, Fang, Jing
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 20.04.2012; Public Library of Science (PLoS)
• Subjects: Apoptosis; Biology; Cell Nucleus - genetics; Cell Nucleus - metabolism; Cloning; Clusterin; Clusterin - genetics; Clusterin - metabolism; Colorectal cancer; Cysts; Gene expression; HEK293 Cells; Humans; Hypoxia; Hypoxia-Inducible Factor 1, alpha Subunit - genetics; Hypoxia-Inducible Factor 1, alpha Subunit - metabolism; Hypoxia-inducible factors; Kinases; Laboratories; Ligases; Medicine; Metabolism; Neoplasia; Nuclear transport; Nutrition; Penicillin; Phosphatase; Prostate cancer; Proteasome Endopeptidase Complex - genetics; Proteasome Endopeptidase Complex - metabolism; Proteasomes; Protein binding; Proteins; Recognition; RNA polymerase; Translocation; Tumor suppressor genes; Tumors; Ubiquitin; Ubiquitin-protein ligase; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; Ubiquitination; Ubiquitination - physiology; VHL protein; Von Hippel-Lindau Tumor Suppressor Protein - genetics; Von Hippel-Lindau Tumor Suppressor Protein - metabolism; China

pVHL, product of von Hippel-Lindau (VHL) tumor suppressor gene, functions as the substrate recognition component of an E3-ubiquitin ligase that targets proteins for ubiquitination and proteasomal degradation. Hypoxia-inducible factor α (HIFα) is the well-known substrate of pVHL. Besides HIFα, pVHL a...