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10.1073/pnas.181341498 http://scihub22266oqcxt.onion/10.1073/pnas.181341498 11504942!55503!11504942     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2001 ; 98 (17): 9630-5 Nephropedia Template TP {{tp|p=11504942|t=2001. HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation |pdf=|usr=}}{{11504942}} gab.com Text HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=11504942 #FOAvip Hypoxia-inducible factor-1alpha (HIF-1alpha) is a global transcriptional regulator of the hypoxic response. Under normoxic conditions, HIF-1alpha is recognized by the von Hippel-Lindau tumor-suppressor protein (VHL), a component of an E3 ubiquitin ligase complex. This interaction thereby promotes the rapid degradation of HIF-1alpha. Under hypoxic conditions, HIF-1alpha is stabilized. We have previously shown that VHL binds in a hypoxia-sensitive manner to a 27-aa segment of HIF-1alpha, and that this regulation depends on a posttranslational modification of HIF-1alpha. Through a combination of in vivo coimmunoprecipitation assays using VHL and a panel of point mutants of HIF-1alpha in this region, as well as MS and in vitro binding assays, we now provide evidence that this modification, which occurs under normoxic conditions, is hydroxylation of Pro-564 of HIF-1alpha. The data furthermore show that this proline hydroxylation is the primary regulator of VHL binding. Twit Text FOAVip HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=11504942 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=11504942 #FOAvip English Wikipedia <ref>{{Cite pmid|11504942}}</ref> HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation #MMPMID11504942 Yu F; White SB; Zhao Q; Lee FS Proc Natl Acad Sci U S A 2001[Aug]; 98 (17): 9630-5 PMID11504942show ga Hypoxia-inducible factor-1alpha (HIF-1alpha) is a global transcriptional regulator of the hypoxic response. Under normoxic conditions, HIF-1alpha is recognized by the von Hippel-Lindau tumor-suppressor protein (VHL), a component of an E3 ubiquitin ligase complex. This interaction thereby promotes the rapid degradation of HIF-1alpha. Under hypoxic conditions, HIF-1alpha is stabilized. We have previously shown that VHL binds in a hypoxia-sensitive manner to a 27-aa segment of HIF-1alpha, and that this regulation depends on a posttranslational modification of HIF-1alpha. Through a combination of in vivo coimmunoprecipitation assays using VHL and a panel of point mutants of HIF-1alpha in this region, as well as MS and in vitro binding assays, we now provide evidence that this modification, which occurs under normoxic conditions, is hydroxylation of Pro-564 of HIF-1alpha. The data furthermore show that this proline hydroxylation is the primary regulator of VHL binding. |*Ligases[MESH] |*Protein Processing, Post-Translational[MESH] |*Transcription Factors[MESH] |*Tumor Suppressor Proteins[MESH] |*Ubiquitin-Protein Ligases[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |COS Cells[MESH] |Cell Hypoxia[MESH] |Chlorocebus aethiops[MESH] |Cobalt/pharmacology[MESH] |DNA-Binding Proteins/*metabolism[MESH] |HeLa Cells[MESH] |Humans[MESH] |Hydroxylation[MESH] |Hydroxyproline/chemistry/*physiology[MESH] |Hypoxia-Inducible Factor 1[MESH] |Hypoxia-Inducible Factor 1, alpha Subunit[MESH] |Macromolecular Substances[MESH] |Molecular Sequence Data[MESH] |Nuclear Proteins/*metabolism[MESH] |Peptide Fragments/metabolism[MESH] |Point Mutation[MESH] |Proline/chemistry[MESH] |Protein Binding/drug effects[MESH] |Proteins/genetics/*metabolism[MESH] |Recombinant Fusion Proteins/chemistry/metabolism[MESH] |Transfection[MESH]HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline (epmc).pdf DeepDyve Pubget Overpricing