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http://purl.uniprot.org/citations/21835666http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21835666http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21835666http://www.w3.org/2000/01/rdf-schema#comment"Tail-anchored (TA) proteins access the secretory pathway via posttranslational insertion of their C-terminal transmembrane domain into the endoplasmic reticulum (ER). Get3 is an ATPase that delivers TA proteins to the ER by interacting with the Get1-Get2 transmembrane complex, but how Get3's nucleotide cycle drives TA protein insertion remains unclear. Here, we establish that nucleotide binding to Get3 promotes Get3-TA protein complex formation by recruiting Get3 to a chaperone that hands over TA proteins to Get3. Biochemical reconstitution and mutagenesis reveal that the Get1-Get2 complex comprises the minimal TA protein insertion machinery with functionally critical cytosolic regions. By engineering a soluble heterodimer of Get1-Get2 cytosolic domains, we uncover the mechanism of TA protein release from Get3: Get2 tethers Get3-TA protein complexes into proximity with the ATPase-dependent, substrate-releasing activity of Get1. Lastly, we show that ATP enhances Get3 dissociation from the membrane, thus freeing Get1-Get2 for new rounds of substrate insertion."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2011.07.020"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2011.07.020"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Denic V."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Denic V."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Tung M."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Tung M."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Whynot A."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/author"Whynot A."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/pages"738-750"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/pages"738-750"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/title"The mechanism of tail-anchored protein insertion into the ER membrane."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/title"The mechanism of tail-anchored protein insertion into the ER membrane."xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/21835666http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/21835666http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21835666
http://purl.uniprot.org/citations/21835666http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21835666