Source:http://linkedlifedata.com/resource/pubmed/id/18343407
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-4-3
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1089-8638
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
378
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
145-53
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pubmed:meshHeading |
pubmed-meshheading:18343407-Amino Acid Sequence,
pubmed-meshheading:18343407-Animals,
pubmed-meshheading:18343407-Cadherins,
pubmed-meshheading:18343407-Cattle,
pubmed-meshheading:18343407-Cytoplasm,
pubmed-meshheading:18343407-Humans,
pubmed-meshheading:18343407-Kidney,
pubmed-meshheading:18343407-Molecular Sequence Data,
pubmed-meshheading:18343407-Protein Interaction Mapping,
pubmed-meshheading:18343407-alpha-Crystallin B Chain
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pubmed:year |
2008
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pubmed:articleTitle |
alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16.
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pubmed:affiliation |
Section for Transplantation Immunology and Immunohematology, Center for Medical Research, University Medical Clinic, Waldhörnlestrasse 22, D-72072 Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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