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10.1242/jcs.186148 http://scihub22266oqcxt.onion/10.1242/jcs.186148 C4920254!4920254!27142834     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27142834&cmd=llinks): Failed to open stream: HTTP request failed! 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The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell?cell trans-dimerization of Na,K-ATPase ?1 subunits |pdf=|usr=}}{{27142834}} gab.com Text The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell cell trans-dimerization of Na,K-ATPase 1 subunits JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=27142834 #FOAvip FXYD5 (also known as dysadherin), a regulatory subunit of the Na,K-ATPase, impairs intercellular adhesion by a poorly understood mechanism. Here, we determined whether FXYD5 disrupts the trans-dimerization of Na,K-ATPase molecules located in neighboring cells. Mutagenesis of the Na,K-ATPase ?1 subunit identified four conserved residues, including Y199, that are crucial for the intercellular Na,K-ATPase trans-dimerization and adhesion. Modulation of expression of FXYD5 or of the ?1 subunit with intact or mutated ?1??1 binding sites demonstrated that the anti-adhesive effect of FXYD5 depends on the presence of Y199 in the ?1 subunit. Immunodetection of the plasma membrane FXYD5 was prevented by the presence of O-glycans. Partial FXYD5 deglycosylation enabled antibody binding and showed that the protein level and the degree of O-glycosylation were greater in cancer than in normal cells. FXYD5-induced impairment of adhesion was abolished by both genetic and pharmacological inhibition of FXYD5 O-glycosylation. Therefore, the extracellular O-glycosylated domain of FXYD5 impairs adhesion by interfering with intercellular ?1??1 interactions, suggesting that the ratio between FXYD5 and ?1??1 heterodimer determines whether the Na,K-ATPase acts as a positive or negative regulator of intercellular adhesion. Twit Text FOAVip The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell cell trans-dimerization of Na,K-ATPase 1 subunits ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=27142834 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27142834 #FOAvip English Wikipedia <ref>{{Cite pmid|27142834}}</ref> The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell?cell trans-dimerization of Na,K-ATPase ?1 subunits #MMPMID27142834 Tokhtaeva E; Sun H; Deiss-Yehiely N; Wen Y; Soni PN; Gabrielli NM; Marcus EA; Ridge KM; Sachs G; Vazquez-Levin M; Sznajder JI; Vagin O; Dada LA J Cell Sci 2016[Jun]; 129 (12): 2394-406 PMID27142834show ga FXYD5 (also known as dysadherin), a regulatory subunit of the Na,K-ATPase, impairs intercellular adhesion by a poorly understood mechanism. Here, we determined whether FXYD5 disrupts the trans-dimerization of Na,K-ATPase molecules located in neighboring cells. Mutagenesis of the Na,K-ATPase ?1 subunit identified four conserved residues, including Y199, that are crucial for the intercellular Na,K-ATPase trans-dimerization and adhesion. Modulation of expression of FXYD5 or of the ?1 subunit with intact or mutated ?1??1 binding sites demonstrated that the anti-adhesive effect of FXYD5 depends on the presence of Y199 in the ?1 subunit. Immunodetection of the plasma membrane FXYD5 was prevented by the presence of O-glycans. Partial FXYD5 deglycosylation enabled antibody binding and showed that the protein level and the degree of O-glycosylation were greater in cancer than in normal cells. FXYD5-induced impairment of adhesion was abolished by both genetic and pharmacological inhibition of FXYD5 O-glycosylation. Therefore, the extracellular O-glycosylated domain of FXYD5 impairs adhesion by interfering with intercellular ?1??1 interactions, suggesting that the ratio between FXYD5 and ?1??1 heterodimer determines whether the Na,K-ATPase acts as a positive or negative regulator of intercellular adhesion. äThe O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting (epmc).pdf DeepDyve Pubget Overpricing