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10.1242/jcs.153437 http://scihub22266oqcxt.onion/10.1242/jcs.153437 C4197088!4197088!25179596     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25179596.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Sci 2014 ; 127 (20): 4457-69 Nephropedia Template TP {{tp|p=25179596|t=2014. Galectin-4-mediated transcytosis of transferrin receptor |pdf=|usr=}}{{25179596}} gab.com Text Galectin-4-mediated transcytosis of transferrin receptor JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=25179596 #FOAvip Some native epithelia, for example, retinal pigment epithelium (RPE) and kidney proximal tubule (KPT), constitutively lack the basolateral sorting adaptor AP-1B; this results in many basolateral plasma membrane proteins being repositioned to the apical domain, where they perform essential functions for their host organs. We recently reported the underlying apical polarity reversal mechanism: in the absence of AP-1B-mediated basolateral sorting, basolateral proteins are shuttled to the apical plasma membrane through a transcytotic pathway mediated by the plus-end kinesin KIF16B. Here, we demonstrate that this apical transcytotic pathway requires apical sorting of basolateral proteins, which is mediated by apical signals and galectin-4. Using RPE and KPT cell lines, and AP-1B-knockdown MDCK cells, we show that mutation of the N-glycan linked to N727 in the basolateral marker transferrin receptor (TfR) or knockdown of galectin-4 inhibits TfR transcytosis to apical recycling endosomes and the apical plasma membrane, and promotes TfR lysosomal targeting and subsequent degradation. Our results report a new role of galectins in basolateral to apical epithelial transcytosis. Twit Text FOAVip Galectin-4-mediated transcytosis of transferrin receptor ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=25179596 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25179596 #FOAvip English Wikipedia <ref>{{Cite pmid|25179596}}</ref> Galectin-4-mediated transcytosis of transferrin receptor #MMPMID25179596 Perez Bay AE; Schreiner R; Benedicto I; Rodriguez-Boulan EJ J Cell Sci 2014[Oct]; 127 (20): 4457-69 PMID25179596show ga Some native epithelia, for example, retinal pigment epithelium (RPE) and kidney proximal tubule (KPT), constitutively lack the basolateral sorting adaptor AP-1B; this results in many basolateral plasma membrane proteins being repositioned to the apical domain, where they perform essential functions for their host organs. We recently reported the underlying apical polarity reversal mechanism: in the absence of AP-1B-mediated basolateral sorting, basolateral proteins are shuttled to the apical plasma membrane through a transcytotic pathway mediated by the plus-end kinesin KIF16B. Here, we demonstrate that this apical transcytotic pathway requires apical sorting of basolateral proteins, which is mediated by apical signals and galectin-4. Using RPE and KPT cell lines, and AP-1B-knockdown MDCK cells, we show that mutation of the N-glycan linked to N727 in the basolateral marker transferrin receptor (TfR) or knockdown of galectin-4 inhibits TfR transcytosis to apical recycling endosomes and the apical plasma membrane, and promotes TfR lysosomal targeting and subsequent degradation. Our results report a new role of galectins in basolateral to apical epithelial transcytosis. äGalectin-4-mediated transcytosis of transferrin receptor (epmc).pdf DeepDyve Pubget Overpricing