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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 PMID27142834 show 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. |*Protein Multimerization [MESH] |A549 Cells [MESH] |Amino Acids/metabolism [MESH] |Animals [MESH] |Antibody Specificity [MESH] |Cell Adhesion [MESH] |Cell Line, Tumor [MESH] |Cell Membrane/metabolism [MESH] |Dogs [MESH] |Epithelial Cells/metabolism [MESH] |Gene Knockdown Techniques [MESH] |Glycosylation [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Ion Channels [MESH] |Madin Darby Canine Kidney Cells [MESH] |Membrane Glycoproteins/*metabolism [MESH] |Mice [MESH] |Microfilament Proteins [MESH] |Neoplasm Proteins/*metabolism [MESH] |Protein Binding [MESH] |Protein Subunits/chemistry/*metabolism [MESH] |Rats [MESH]The O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting (epmc).pdf DeepDyve Pubget Overpricing