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http://purl.uniprot.org/citations/17189291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17189291http://www.w3.org/2000/01/rdf-schema#comment"Calsenilin/DREAM/KChIP3, a neuronal Ca(2+)-binding protein, has multifunctions in nucleus and cytosol. Here, we identified CLN3 as a calsenilin-binding partner whose mutation or deletion is observed in Batten disease. In vitro binding and immunoprecipitation assays show that calsenilin interacts with the C-terminal region of CLN3 and the increase of Ca(2+) concentration in vitro and in cells causes significant dissociation of calsenilin from CLN3. Ectopic expression of CLN3 or its deletion mutant containing only the C-terminus (153-438) and capable of binding to calsenilin suppresses thapsigargin or A23187-induced death of neuronal cells. In contrast, CLN3 deletion mutant containing the N-terminus (1-153) or (1-263), which is frequently found in Batten disease, induces the perturbation of Ca(2+) transient and fails to inhibit the cell death. In addition, the expression of calsenilin is increased in the brain tissues of CLN3 knock-out mice and SH-SY5Y/CLN3 knock-down cells. Down-regulation of CLN3 expression sensitizes SH-SY5Y cells to thapsigargin or A23187. However, additional decrease of calsenilin expression rescues the sensitivity of SH-SY5Y/CLN3 knock-down cells to Ca(2+)-mediated cell death. These results suggest that the vulnerability of CLN3 knock-out or CLN3 deletion (1-153)-expressing neuronal cells to Ca(2+)-induced cell death may be mediated by calsenilin."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.org/dc/terms/identifier"doi:10.1093/hmg/ddl466"xsd:string
http://purl.uniprot.org/citations/17189291http://purl.org/dc/terms/identifier"doi:10.1093/hmg/ddl466"xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Kim H.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Kim H.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Choi H."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Choi H."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Park W.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Park W.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jeon Y.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jeon Y.J."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jung Y.K."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jung Y.K."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Noh J.Y."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Noh J.Y."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Chang J.W."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Chang J.W."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jo D.G."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/author"Jo D.G."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string
http://purl.uniprot.org/citations/17189291http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string