| http://purl.uniprot.org/citations/18343407 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18343407 | http://www.w3.org/2000/01/rdf-schema#comment | "The Ca(2+)-dependent membrane-spanning classical cadherins bind directly to cytosolic catenins. This cadherin-catenin interaction is known to be critical for the fundamental role of cadherins in cell-cell adhesion. The small subfamily of the 7D-cadherins, however, cannot interact with catenins due to their highly truncated cytoplasmic tail. Thus far, no cytoplasmic interaction partner for the 7D-cadherins has been described. With the use of the cytoplasmic domain of the Ksp (kidney-specific)-cadherin, which belongs to the family of 7D-cadherins, as bait in affinity chromatography with human kidney lysates, the small heat-shock protein alpha B-crystallin was identified by matrix-assisted laser desorption/ionization-time-of-flight analysis as a cytosolic binding partner of Ksp-cadherin. This interaction was verified by co-immunoprecipitation analysis. With the use of overlapping peptides representing the entire alpha B-crystallin molecule, the N-terminal part of alpha B-crystallin, which does not possess chaperone activity, was identified as responsible for the binding to Ksp-cadherin. This interaction was found to be specific since only the cytoplasmic domain of Ksp-cadherin, but not LI (liver-intestine)-cadherin (another member of the 7D-cadherin family), interacted with alpha B-crystallin. In the human kidney, both alpha B-crystallin and Ksp-cadherin co-localize to cells of the collecting duct. They also co-localize with the actin cytoskeleton and co-precipitate with the latter. These findings suggest that the interaction of Ksp-cadherin with alpha B-crystallin is important for the connection of Ksp-cadherin to the cytoskeleton and thus for maintaining tissue integrity in the kidney."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2008.02.008"xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Stevanovic S."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Klein G."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Kratzer U."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Kalbacher H."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Lammers R."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/author | "Thedieck C."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/pages | "145-153"xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/title | "alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16."xsd:string |
| http://purl.uniprot.org/citations/18343407 | http://purl.uniprot.org/core/volume | "378"xsd:string |
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