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Details on Person Inherited mutations in VHL gene result in von Hippel-Lindau ...

Class:IdSummation:391799
_displayNameInherited mutations in VHL gene result in von Hippel-Lindau ...
_timestamp2015-11-27 20:47:42
created[InstanceEdit:391778] Matthews, L, 2009-02-24 06:34:11
literatureReference[LiteratureReference:392077] Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
[LiteratureReference:392094] The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity
[LiteratureReference:392100] The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
[LiteratureReference:392086] von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF
[LiteratureReference:392092] Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
[LiteratureReference:392095] Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
[LiteratureReference:391404] Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
[LiteratureReference:391551] The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
modified[InstanceEdit:391802] Matthews, L, 2009-02-24 06:35:16
[InstanceEdit:392093] Matthews, L, 2009-02-26 19:13:31
[InstanceEdit:392795] Matthews, L, 2009-03-08 07:11:56
[InstanceEdit:6814808] Orlic-Milacic, Marija, 2015-11-27
[InstanceEdit:6814816] Orlic-Milacic, Marija, 2015-11-27
[InstanceEdit:6814822] Orlic-Milacic, Marija, 2015-11-27
textInherited mutations in VHL gene result in von Hippel-Lindau disease, a rare autosomal dominant genetic disorder associated with renal angioma, renal cell carcinoma and pheochromocytoma. VHL encodes a tumor suppressor protein that associates with elongin-B (TCEB2) and elongin C (TCEB1) ( Kibel et al. 1995) to form the VBC complex. The VBC complex is part of a larger SCF-like ubiquitin ligase complex that promotes the destruction of a number of proteins required for growth and vascularization of solid tumors, including the hypoxia-inducible factors (HIFs) (Iwai et al. 1999, Kamura et al. 1999, Lisztwan et al. 1999, Pause et al. 1997, Jaakkola et al. 2001, Ohh et al. 2000). The Hsp70 and TRiC/CCT chaperone systems cooperate to assemble the VBC (Feldman et al. 1999, Melville et al. 2003) and some of the cancer-causing VHL mutations specifically disrupt the interaction with the chaperonin complex, resulting in misfolded VHL (Feldman etal. 2003). For a recent review of the tumor suppressor role of VHL, please refer to Gossage et al. 2015.
(summation)[Pathway:390494] Cooperation of the Hsp70 and TRiC/CCT chaperone systems assembly of the VBC tumor suppressor complex [Homo sapiens]
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