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10.1126/sciadv.aas9184 http://scihub22266oqcxt.onion/10.1126/sciadv.aas9184 C6040840!6040840 !30009260     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\30009260 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Adv 2018 ; 4 (7 ): eaas9184 Nephropedia Template TP {{tp|p=30009260 |t=2018. Phosphorylation of human TRM9L integrates multiple stress-signaling pathways for tumor growth suppression |pdf=|usr=}}{{30009260 }} gab.com Text Phosphorylation of human TRM9L integrates multiple stress-signaling pathways for tumor growth suppression JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=30009260 #FOAvip The human transfer RNA methyltransferase 9-like gene (TRM9L, also known as KIAA1456) encodes a negative regulator of tumor growth that is frequently silenced in many forms of cancer. While TRM9L can inhibit tumor cell growth in vivo, the molecular mechanisms underlying the tumor inhibition activity of TRM9L are unknown. We show that oxidative stress induces the rapid and dose-dependent phosphorylation of TRM9L within an intrinsically disordered domain that is necessary for tumor growth suppression. Multiple serine residues are hyperphosphorylated in response to oxidative stress. Using a chemical genetic approach, we identified a key serine residue in TRM9L that undergoes hyperphosphorylation downstream of the oxidative stress-activated MEK (mitogen-activated protein kinase kinase)-ERK (extracellular signal-regulated kinase)-RSK (ribosomal protein S6 kinase) signaling cascade. Moreover, we found that phosphorylated TRM9L interacts with the 14-3-3 family of proteins, providing a link between oxidative stress and downstream cellular events involved in cell cycle control and proliferation. Mutation of the serine residues required for TRM9L hyperphosphorylation and 14-3-3 binding abolished the tumor inhibition activity of TRM9L. Our results uncover TRM9L as a key downstream effector of the ERK signaling pathway and elucidate a phospho-signaling regulatory mechanism underlying the tumor inhibition activity of TRM9L. Twit Text FOAVip Phosphorylation of human TRM9L integrates multiple stress-signaling pathways for tumor growth suppression ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=30009260 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30009260 #FOAvip English Wikipedia <ref>{{Cite pmid|30009260 }}</ref> Phosphorylation of human TRM9L integrates multiple stress-signaling pathways for tumor growth suppression #MMPMID30009260 Gu C ; Ramos J ; Begley U ; Dedon PC ; Fu D ; Begley TJ Sci Adv 2018[Jul]; 4 (7 ): eaas9184 PMID30009260 show ga The human transfer RNA methyltransferase 9-like gene (TRM9L, also known as KIAA1456) encodes a negative regulator of tumor growth that is frequently silenced in many forms of cancer. While TRM9L can inhibit tumor cell growth in vivo, the molecular mechanisms underlying the tumor inhibition activity of TRM9L are unknown. We show that oxidative stress induces the rapid and dose-dependent phosphorylation of TRM9L within an intrinsically disordered domain that is necessary for tumor growth suppression. Multiple serine residues are hyperphosphorylated in response to oxidative stress. Using a chemical genetic approach, we identified a key serine residue in TRM9L that undergoes hyperphosphorylation downstream of the oxidative stress-activated MEK (mitogen-activated protein kinase kinase)-ERK (extracellular signal-regulated kinase)-RSK (ribosomal protein S6 kinase) signaling cascade. Moreover, we found that phosphorylated TRM9L interacts with the 14-3-3 family of proteins, providing a link between oxidative stress and downstream cellular events involved in cell cycle control and proliferation. Mutation of the serine residues required for TRM9L hyperphosphorylation and 14-3-3 binding abolished the tumor inhibition activity of TRM9L. Our results uncover TRM9L as a key downstream effector of the ERK signaling pathway and elucidate a phospho-signaling regulatory mechanism underlying the tumor inhibition activity of TRM9L. |*Oxidative Stress/drug effects [MESH] |*Signal Transduction/drug effects [MESH] |14-3-3 Proteins/metabolism [MESH] |Amino Acid Sequence [MESH] |Cell Line, Tumor [MESH] |Cell Proliferation/drug effects [MESH] |Extracellular Signal-Regulated MAP Kinases/metabolism [MESH] |Humans [MESH] |Hydrogen Peroxide/pharmacology [MESH] |MAP Kinase Kinase Kinases/metabolism [MESH] |Neoplasms/metabolism/pathology [MESH] |Phosphopeptides/analysis [MESH] |Phosphorylation/drug effects [MESH] |Protein Kinase Inhibitors/pharmacology [MESH] |Ribosomal Protein S6 Kinases/metabolism [MESH] |Tandem Mass Spectrometry [MESH]Phosphorylation of human TRM9L integrates multiple stress-signaling pa(epmc).pdf DeepDyve Pubget Overpricing