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10.1038/cr.2015.90 http://scihub22266oqcxt.onion/10.1038/cr.2015.90 C4559813!4559813!26215701     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Res 2015 ; 25 (9): 1025-42 Nephropedia Template TP {{tp|p=26215701|t=2015. RHOBTB3 promotes proteasomal degradation of HIF? through facilitating hydroxylation and suppresses the Warburg effect |pdf=|usr=}}{{26215701}} gab.com Text RHOBTB3 promotes proteasomal degradation of HIF through facilitating hydroxylation and suppresses the Warburg effect JO: Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=26215701 #FOAvip Hypoxia-inducible factors (HIFs) are master regulators of adaptive responses to low oxygen, and their ?-subunits are rapidly degraded through the ubiquitination-dependent proteasomal pathway after hydroxylation. Aberrant accumulation or activation of HIFs is closely linked to many types of cancer. However, how hydroxylation of HIF? and its delivery to the ubiquitination machinery are regulated remains unclear. Here we show that Rho-related BTB domain-containing protein 3 (RHOBTB3) directly interacts with the hydroxylase PHD2 to promote HIF? hydroxylation. RHOBTB3 also directly interacts with the von Hippel-Lindau (VHL) protein, a component of the E3 ubiquitin ligase complex, facilitating ubiquitination of HIF?. Remarkably, RHOBTB3 dimerizes with LIMD1, and constructs a RHOBTB3/LIMD1-PHD2-VHL-HIF? complex to effect the maximal degradation of HIF?. Hypoxia reduces the RHOBTB3-centered complex formation, resulting in an accumulation of HIF?. Importantly, the expression level of RHOBTB3 is greatly reduced in human renal carcinomas, and RHOBTB3 deficiency significantly elevates the Warburg effect and accelerates xenograft growth. Our work thus reveals that RHOBTB3 serves as a scaffold to organize a multi-subunit complex that promotes the hydroxylation, ubiquitination and degradation of HIF?. Twit Text FOAVip RHOBTB3 promotes proteasomal degradation of HIF through facilitating hydroxylation and suppresses the Warburg effect ????Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=26215701 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26215701 #FOAvip English Wikipedia <ref>{{Cite pmid|26215701}}</ref> RHOBTB3 promotes proteasomal degradation of HIF? through facilitating hydroxylation and suppresses the Warburg effect #MMPMID26215701 Zhang CS; Liu Q; Li M; Lin SY; Peng Y; Wu D; Li TY; Fu Q; Jia W; Wang X; Ma T; Zong Y; Cui J; Pu C; Lian G; Guo H; Ye Z; Lin SC Cell Res 2015[Sep]; 25 (9): 1025-42 PMID26215701show ga Hypoxia-inducible factors (HIFs) are master regulators of adaptive responses to low oxygen, and their ?-subunits are rapidly degraded through the ubiquitination-dependent proteasomal pathway after hydroxylation. Aberrant accumulation or activation of HIFs is closely linked to many types of cancer. However, how hydroxylation of HIF? and its delivery to the ubiquitination machinery are regulated remains unclear. Here we show that Rho-related BTB domain-containing protein 3 (RHOBTB3) directly interacts with the hydroxylase PHD2 to promote HIF? hydroxylation. RHOBTB3 also directly interacts with the von Hippel-Lindau (VHL) protein, a component of the E3 ubiquitin ligase complex, facilitating ubiquitination of HIF?. Remarkably, RHOBTB3 dimerizes with LIMD1, and constructs a RHOBTB3/LIMD1-PHD2-VHL-HIF? complex to effect the maximal degradation of HIF?. Hypoxia reduces the RHOBTB3-centered complex formation, resulting in an accumulation of HIF?. Importantly, the expression level of RHOBTB3 is greatly reduced in human renal carcinomas, and RHOBTB3 deficiency significantly elevates the Warburg effect and accelerates xenograft growth. Our work thus reveals that RHOBTB3 serves as a scaffold to organize a multi-subunit complex that promotes the hydroxylation, ubiquitination and degradation of HIF?. äRHOBTB3 promotes proteasomal degradation of HIF? through facilitating (epmc).pdf DeepDyve Pubget Overpricing