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VHL (タンパク質)

出典: フリー百科事典『ウィキペディア（Wikipedia）』 (2021/06/01 10:19 UTC 版)

VHLタンパク質またはvon Hippel-Lindau腫瘍抑制因子（von Hippel-Lindau tumor suppressor）は、ヒトではVHL遺伝子にコードされるタンパク質である。VHL遺伝子の変異は、フォン・ヒッペル・リンドウ病（VHL病）と関係している^[5]。疾患名などと区別するため、pVHLと書かれることもある。

出典

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000134086 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000033933 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
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^ “Entrez Gene: VHL von Hippel–Lindau tumor suppressor”. 2019年11月9日閲覧。
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^ ^a ^b Maxwell, Patrick H. (2005-8). “The HIF pathway in cancer”. Seminars in Cell & Developmental Biology 16 (4-5): 523–530. doi:10.1016/j.semcdb.2005.03.001. ISSN 1084-9521. PMID 16144689.
^ “Heterogeneous Effects of Direct Hypoxia Pathway Activation in Kidney Cancer”. PLoS One 10 (8): e0134645. (2015). doi:10.1371/journal.pone.0134645. PMC: 4532367. PMID 26262842.
^ ^a ^b ^c ^d ^e “The von Hippel–Lindau tumor suppressor protein and clear cell renal carcinoma”. Clinical Cancer Research 13 (2 Pt 2): 680s–684s. (January 2007). doi:10.1158/1078-0432.CCR-06-1865. PMID 17255293.
^ “Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex”. Genes & Development 18 (23): 2893–904. (December 2004). doi:10.1101/gad.1256804. PMC: 534650. PMID 15545625.
^ ^a ^b “Molecular basis of the VHL hereditary cancer syndrome”. Nature Reviews. Cancer 2 (9): 673–82. (September 2002). doi:10.1038/nrc885. PMID 12209156.
^ “The von Hippel–Lindau tumor suppressor protein influences microtubule dynamics at the cell periphery”. Experimental Cell Research 301 (2): 139–46. (December 2004). doi:10.1016/j.yexcr.2004.07.016. PMID 15530850.
^ “Cardiopulmonary function in two human disorders of the hypoxia-inducible factor (HIF) pathway: von Hippel–Lindau disease and HIF-2alpha gain-of-function mutation”. FASEB Journal 25 (6): 2001–11. (June 2011). doi:10.1096/fj.10-177378. PMC: 3159892. PMID 21389259.
^ “Effect of ascorbate on the activity of hypoxia-inducible factor in cancer cells”. Cancer Research 63 (8): 1764–8. (April 2003). PMID 12702559.
^ ^a ^b ^c “Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome”. BMC Biochemistry 9: 1. (2008). doi:10.1186/1471-2091-9-1. PMC: 2265268. PMID 18173839.
^ ^a ^b ^c “Large-scale mapping of human protein-protein interactions by mass spectrometry”. Molecular Systems Biology 3: 89. (2007). doi:10.1038/msb4100134. PMC: 1847948. PMID 17353931.
^ ^a ^b ^c “Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel–Lindau protein”. The Journal of Clinical Investigation 104 (11): 1583–91. (December 1999). doi:10.1172/JCI8161. PMC: 481054. PMID 10587522.
^ ^a ^b ^c Zhang, Baohong, ed (2008). “VHL type 2B mutations retain VBC complex form and function”. PLoS One 3 (11): e3801. doi:10.1371/journal.pone.0003801. PMC: 2583047. PMID 19030229.
^ “Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase”. The Journal of Biological Chemistry 276 (32): 29748–53. (August 2001). doi:10.1074/jbc.M103093200. PMID 11384984.
^ ^a ^b “The von Hippel–Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1”. The Journal of Biological Chemistry 277 (42): 39887–98. (October 2002). doi:10.1074/jbc.M205040200. PMID 12169691.
^ ^a ^b “Identification of a novel protein (VBP-1) binding to the von Hippel–Lindau (VHL) tumor suppressor gene product”. Cancer Research 56 (13): 2881–5. (July 1996). PMID 8674032.
^ ^a ^b “FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity”. Genes & Development 15 (20): 2675–86. (October 2001). doi:10.1101/gad.924501. PMC: 312814. PMID 11641274.
^ ^a ^b ^c “Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation”. Experimental & Molecular Medicine 40 (1): 71–83. (February 2008). doi:10.3858/emm.2008.40.1.71. PMC: 2679322. PMID 18305400.
^ ^a ^b ^c “Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling”. Science 296 (5574): 1886–9. (June 2002). doi:10.1126/science.1073440. PMID 12004076.
^ ^a ^b “Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel–Lindau protein”. Nature Genetics 35 (3): 229–37. (November 2003). doi:10.1038/ng1254. PMID 14556007.
^ “The VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activity”. The EMBO Journal 22 (8): 1857–67. (April 2003). doi:10.1093/emboj/cdg173. PMC: 154465. PMID 12682018.
^ “Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel–Lindau tumor suppressor protein”. The EMBO Journal 19 (16): 4298–309. (August 2000). doi:10.1093/emboj/19.16.4298. PMC: 302039. PMID 10944113.
^ “HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation”. Proceedings of the National Academy of Sciences of the United States of America 98 (17): 9630–5. (August 2001). doi:10.1073/pnas.181341498. PMC: 55503. PMID 11504942.
^ “STAT3 inhibits the degradation of HIF-1alpha by pVHL-mediated ubiquitination”. Experimental & Molecular Medicine 40 (5): 479–85. (October 2008). doi:10.3858/emm.2008.40.5.479. PMC: 2679355. PMID 18985005.
^ “Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha”. The Journal of Biological Chemistry 283 (43): 29375–84. (October 2008). doi:10.1074/jbc.M805919200. PMC: 2662024. PMID 18694926.
^ “Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel–Lindau recruitment and asparagine hydroxylation”. Molecular Pharmacology 74 (1): 236–45. (July 2008). doi:10.1124/mol.108.045278. PMID 18426857.
^ ^a ^b “Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel–Lindau tumor suppressor protein”. The Journal of Biological Chemistry 277 (7): 4656–62. (February 2002). doi:10.1074/jbc.M108269200. PMID 11739384.

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