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10.1016/j.devcel.2014.07.021 http://scihub22266oqcxt.onion/10.1016/j.devcel.2014.07.021 C4203341!4203341!25241935     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Dev+Cell 2014 ; 30 (6): 688-700 Nephropedia Template TP {{tp|p=25241935|t=2014. Trim58 degrades dynein and regulates terminal erythropoiesis |pdf=|usr=}}{{25241935}} gab.com Text Trim58 degrades dynein and regulates terminal erythropoiesis JO: Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=25241935 #FOAvip TRIM58 is an E3 ubiquitin ligase superfamily member implicated by genome wide association studies (GWAS) to regulate human erythrocyte traits. Here we show that Trim58 expression is induced during late erythropoiesis and that its depletion by shRNAs inhibits the maturation of late stage nucleated erythroblasts to anucleate reticulocytes. Imaging flow cytometry studies demonstrate that Trim58 regulates polarization and/or extrusion of erythroblast nuclei. In vitro, Trim58 directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein. In cells, Trim58 stimulates proteasome-dependent degradation of the dynein holoprotein complex. During erythropoiesis, Trim58 expression, dynein loss and enucleation occur concomitantly and all are inhibited by Trim58 shRNAs. Dynein regulates nuclear positioning and microtubule organization, both of which undergo dramatic changes during erythroblast enucleation. Thus, we propose that Trim58 regulates this process by eliminating dynein. Our findings identify an erythroid-specific regulator of enucleation and elucidate a previously unrecognized mechanism for controlling dynein activity. Twit Text FOAVip Trim58 degrades dynein and regulates terminal erythropoiesis ????Dev Cell http://www.kidney.de/pget.php?&tw=1&pmid=25241935 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25241935 #FOAvip English Wikipedia <ref>{{Cite pmid|25241935}}</ref> Trim58 degrades dynein and regulates terminal erythropoiesis #MMPMID25241935 Thom CS; Traxler EA; Khandros E; Nickas JM; Zhou OY; Lazarus JE; Silva AP; Prabhu D; Yao Y; Aribeana C; Fuchs SY; Mackay JP; Holzbaur EL; Weiss MJ Dev Cell 2014[Sep]; 30 (6): 688-700 PMID25241935show ga TRIM58 is an E3 ubiquitin ligase superfamily member implicated by genome wide association studies (GWAS) to regulate human erythrocyte traits. Here we show that Trim58 expression is induced during late erythropoiesis and that its depletion by shRNAs inhibits the maturation of late stage nucleated erythroblasts to anucleate reticulocytes. Imaging flow cytometry studies demonstrate that Trim58 regulates polarization and/or extrusion of erythroblast nuclei. In vitro, Trim58 directly binds and ubiquitinates the intermediate chain of the microtubule motor dynein. In cells, Trim58 stimulates proteasome-dependent degradation of the dynein holoprotein complex. During erythropoiesis, Trim58 expression, dynein loss and enucleation occur concomitantly and all are inhibited by Trim58 shRNAs. Dynein regulates nuclear positioning and microtubule organization, both of which undergo dramatic changes during erythroblast enucleation. Thus, we propose that Trim58 regulates this process by eliminating dynein. Our findings identify an erythroid-specific regulator of enucleation and elucidate a previously unrecognized mechanism for controlling dynein activity. äTrim58 degrades dynein and regulates terminal erythropoiesis (epmc).pdf DeepDyve Pubget Overpricing