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http://purl.uniprot.org/citations/29242231http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29242231http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29242231http://www.w3.org/2000/01/rdf-schema#comment"Insertion of proteins into membranes is an essential cellular process. The extensive biophysical and topological diversity of membrane proteins necessitates multiple insertion pathways that remain incompletely defined. Here we found that known membrane insertion pathways fail to effectively engage tail-anchored membrane proteins with moderately hydrophobic transmembrane domains. These proteins are instead shielded in the cytosol by calmodulin. Dynamic release from calmodulin allowed sampling of the endoplasmic reticulum (ER), where the conserved ER membrane protein complex (EMC) was shown to be essential for efficient insertion in vitro and in cells. Purified EMC in synthetic liposomes catalyzed the insertion of its substrates in a reconstituted system. Thus, EMC is a transmembrane domain insertase, a function that may explain its widely pleiotropic membrane-associated phenotypes across organisms."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.org/dc/terms/identifier"doi:10.1126/science.aao3099"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.org/dc/terms/identifier"doi:10.1126/science.aao3099"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Hegde R.S."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Hegde R.S."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Guna A."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Guna A."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Christianson J.C."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Christianson J.C."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Volkmar N."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/author"Volkmar N."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/pages"470-473"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/pages"470-473"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/title"The ER membrane protein complex is a transmembrane domain insertase."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/title"The ER membrane protein complex is a transmembrane domain insertase."xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/volume"359"xsd:string
http://purl.uniprot.org/citations/29242231http://purl.uniprot.org/core/volume"359"xsd:string
http://purl.uniprot.org/citations/29242231http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29242231
http://purl.uniprot.org/citations/29242231http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/29242231