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10.1128/MCB.00142-17 http://scihub22266oqcxt.onion/10.1128/MCB.00142-17 C5640814!5640814!28760776     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell+Biol 2017 ; 37 (21): ä Nephropedia Template TP {{tp|p=28760776|t=2017. TIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Their Nuclear Translocation |pdf=|usr=}}{{28760776}} gab.com Text TIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Their Nuclear Translocation JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28760776 #FOAvip DNA repair pathways are aberrant in cancer, enabling tumor cells to survive standard therapies?chemotherapy and radiotherapy. Our group previously reported that, upon irradiation, the membrane-bound tyrosine kinase receptor TIE2 translocates into the nucleus and phosphorylates histone H4 at Tyr51, recruiting ABL1 to the DNA repair complexes that participate in the nonhomologous end-joining pathway. However, no specific molecular mechanisms of TIE2 endocytosis have been reported. Here, we show that irradiation or ligand-induced TIE2 trafficking is dependent on caveolin-1, the main component of caveolae. Subcellular fractionation and confocal microscopy demonstrated TIE2/caveolin-1 complexes in the nucleus, and using inhibitor or small interfering RNAs (siRNAs) against caveolin-1 or Tie2 inhibited their trafficking. TIE2 was found in caveolae and directly phosphorylated caveolin-1 at Tyr14 in vitro and in vivo. This modification regulated the generation of TIE2/caveolin-1 complexes and was essential for TIE2/caveolin-1 nuclear translocation. Our data further demonstrate that the combination of TIE2 and caveolin-1 inhibitors resulted in significant radiosensitization of malignant glioma cells, which will guide the development of combinatorial treatment with radiotherapy for patients with glioblastoma. Twit Text FOAVip TIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Their Nuclear Translocation ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28760776 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28760776 #FOAvip English Wikipedia <ref>{{Cite pmid|28760776}}</ref> TIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Their Nuclear Translocation #MMPMID28760776 Hossain MB; Shifat R; Li J; Luo X; Hess KR; Rivera-Molina Y; Puerta Martinez F; Jiang H; Lang FF; Hung MC; Fueyo J; Gomez-Manzano C Mol Cell Biol 2017[Nov]; 37 (21): ä PMID28760776show ga DNA repair pathways are aberrant in cancer, enabling tumor cells to survive standard therapies?chemotherapy and radiotherapy. Our group previously reported that, upon irradiation, the membrane-bound tyrosine kinase receptor TIE2 translocates into the nucleus and phosphorylates histone H4 at Tyr51, recruiting ABL1 to the DNA repair complexes that participate in the nonhomologous end-joining pathway. However, no specific molecular mechanisms of TIE2 endocytosis have been reported. Here, we show that irradiation or ligand-induced TIE2 trafficking is dependent on caveolin-1, the main component of caveolae. Subcellular fractionation and confocal microscopy demonstrated TIE2/caveolin-1 complexes in the nucleus, and using inhibitor or small interfering RNAs (siRNAs) against caveolin-1 or Tie2 inhibited their trafficking. TIE2 was found in caveolae and directly phosphorylated caveolin-1 at Tyr14 in vitro and in vivo. This modification regulated the generation of TIE2/caveolin-1 complexes and was essential for TIE2/caveolin-1 nuclear translocation. Our data further demonstrate that the combination of TIE2 and caveolin-1 inhibitors resulted in significant radiosensitization of malignant glioma cells, which will guide the development of combinatorial treatment with radiotherapy for patients with glioblastoma. äTIE2 Associates with Caveolae and Regulates Caveolin-1 To Promote Thei(epmc).pdf DeepDyve Pubget Overpricing