RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/27185316http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27185316http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27185316http://www.w3.org/2000/01/rdf-schema#comment"

Background/aims

Stromal interacting molecule-1 (STIM1) aggregation and redistribution to plasma membrane to interact with Orai1 constitute the core mechanism of store-operated Ca2+ entry (SOCE). Previous study has revealed that calsequestrin-1 (CSQ1) regulates SOCE in HEK293 cells through interacting with STIM1 and inhibiting STIM1/Orai1 interaction. Here, we further investigate how CSQ1/STIM1 interaction affects SOCE.

Methods

Using confocal microscopy, STIM1 aggregation and co-localizations with CSQ1 or Orai1 upon Ca2+ store depletion by thapsigargin were measured and quantified by Imaris software in HeLa cells transfected with different CSQ1 mutants. The interactions of CSQ1/STIM1 and STIM1/Orai1, and internal Ca2+ changes were detected by co-immunoprecipitation and Fura2, respectively.

Results

Wt-CSQ1 overexpression significantly reduced STIM1 clustering in the perimembrane and cytosolic regions, whereas over-expression of a C-terminal amino acid 362-396 deletion mutant (C35) did not. Consistently, a significant depression of SOCE, increased CSQ1 monomerization and CSQ1/STIM1 interaction, and a reduced STIM1/Orai1 association were observed in wt-CSQ1 but not in C35-transfected cells. Additionally, mutant lacking C-terminal AA 388-396 deletion exerted weaker potency in inhibiting STIM1 aggregation and association with Orai1 than wt-CSQ1.

Conclusions

Our results demonstrate that CSQ1 monomers suppress SOCE by interacting with STIM1 and attenuating STIM1 aggregation via its C-terminal amino acid 362-396."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.org/dc/terms/identifier"doi:10.1159/000445574"xsd:string
http://purl.uniprot.org/citations/27185316http://purl.org/dc/terms/identifier"doi:10.1159/000445574"xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Li S."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Luo D."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Luo D."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Xue J."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/author"Xue J."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/name"Cell. Physiol. Biochem."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/name"Cell. Physiol. Biochem."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/pages"2183-2193"xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/pages"2183-2193"xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/title"Calsequestrin-1 regulates store-operated Ca2+ entry by inhibiting STIM1 aggregation."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/title"Calsequestrin-1 regulates store-operated Ca2+ entry by inhibiting STIM1 aggregation."xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/27185316http://purl.uniprot.org/core/volume"38"xsd:string