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http://purl.uniprot.org/citations/27916661http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27916661http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27916661http://www.w3.org/2000/01/rdf-schema#comment"Tetrameric assembly of channel subunits in the endoplasmic reticulum (ER) is essential for surface expression and function of K+ channels, but the molecular mechanism underlying this process remains unclear. In this study, we found through genetic screening that ER-located J-domain-containing chaperone proteins (J-proteins) are critical for the biogenesis and physiological function of ether-a-go-go-related gene (ERG) K+ channels in both Caenorhabditis elegans and human cells. Human J-proteins DNAJB12 and DNAJB14 promoted tetrameric assembly of ERG (and Kv4.2) K+ channel subunits through a heat shock protein (HSP) 70-independent mechanism, whereas a mutated DNAJB12 that did not undergo oligomerization itself failed to assemble ERG channel subunits into tetramers in vitro and in C. elegans. Overexpressing DNAJB14 significantly rescued the defective function of human ether-a-go-go-related gene (hERG) mutant channels associated with long QT syndrome (LQTS), a condition that predisposes to life-threatening arrhythmia, by stabilizing the mutated proteins. Thus, chaperone proteins are required for subunit stability and assembly of K+ channels."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.10.027"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2016.10.027"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Li K."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Li K."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Jiang Q."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Jiang Q."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Yang Y.F."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Yang Y.F."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Bai X."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Bai X."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Cai S.Q."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Cai S.Q."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Ruan M.Y."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/author"Ruan M.Y."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/pages"52-65"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/pages"52-65"xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/title"Tetrameric assembly of K(+) channels requires ER-located chaperone proteins."xsd:string
http://purl.uniprot.org/citations/27916661http://purl.uniprot.org/core/title"Tetrameric assembly of K(+) channels requires ER-located chaperone proteins."xsd:string