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• W2016498245 abstract "Targeting of newly synthesized membrane proteins to the endoplasmic reticulum is an essential cellular process. Most membrane proteins are recognized and targeted co-translationally by the signal recognition particle. However, nearly 5% of membrane proteins are ‘tail-anchored’ by a single carboxy-terminal transmembrane domain that cannot access the co-translational pathway. Instead, tail-anchored proteins are targeted post-translationally by a conserved ATPase termed Get3. The mechanistic basis for tail-anchored protein recognition or targeting by Get3 is not known. Here we present crystal structures of yeast Get3 in ‘open’ (nucleotide-free) and ‘closed’ (ADP·AlF4--bound) dimer states. In the closed state, the dimer interface of Get3 contains an enormous hydrophobic groove implicated by mutational analyses in tail-anchored protein binding. In the open state, Get3 undergoes a striking rearrangement that disrupts the groove and shields its hydrophobic surfaces. These data provide a molecular mechanism for nucleotide-regulated binding and release of tail-anchored proteins during their membrane targeting by Get3. Tail-anchored (TA) proteins mediate essential biochemical processes in nearly every cellular membrane. They are integral membrane proteins containing a cytosolic N-terminal domain anchored to the membrane by a transmembrane domain. Recent studies have suggested that targeting of TA proteins to the endoplasmic reticulum is mediated by the cytosolic ATPase chaperone Get3. The crystal structure of Get3 has now been determined in 'open' nucleotide-free and 'closed' nucleotide-bound forms. The open-to-closed transition results in a substantial conformational change that unveils a large hydrophobic groove sufficient to accommodate TA substrates. These results provide a mechanistic understanding for nucleotide-regulated binding and release of TA proteins. Nearly 5% of membrane proteins are 'tail-anchored' to the endoplasmic reticulum by a single carboxy-terminal transmembrane domain. These tail-anchored proteins are targeted post-translationally by the ATPase Get3, but the mechanism of recognition and targeting by Get3 is not known. Here, the crystal structures of yeast Get3 in a nucleotide-free 'open' state and a nucleotide-bound 'closed' state are presented." @default.
• W2016498245 created "2016-06-24" @default.
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• W2016498245 date "2009-08-12" @default.
• W2016498245 modified "2023-10-01" @default.
• W2016498245 title "The structural basis of tail-anchored membrane protein recognition by Get3" @default.
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• W2016498245 doi "https://doi.org/10.1038/nature08319" @default.
• W2016498245 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6528170" @default.
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• W2016498245 hasPublicationYear "2009" @default.
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