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Published April 2012 | public
Journal Article Open

The complex process of GETting tail-anchored membrane proteins to the ER


Biosynthesis of membrane proteins requires that hydrophobic transmembrane (TM) regions be shielded from the cytoplasm while being directed to the correct membrane. Tail-anchored (TA) membrane proteins, characterized by a single C-terminal TM, pose an additional level of complexity because they must be post-translationally targeted. In eukaryotes, the GET pathway shuttles TA-proteins to the endoplasmic reticulum. The key proteins required in yeast (Sgt2 and Get1–5) have been under extensive structural and biochemical investigation during recent years. The central protein Get3 utilizes nucleotide linked conformational changes to facilitate substrate loading and targeting. Here we analyze this complex process from a structural perspective, as understood in yeast, and further postulate on similar pathways in other domains of life.

Additional Information

© 2012 Elsevier Ltd. Available online 21 March 2012. We are grateful to Harry Gristick, Meera Rao, Doug Rees and Michael Rome for commenting on the manuscript. Research in the Clemons lab is funded by an R01 from the National Institutes of Health grant GM097572.

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Accepted Version - nihms365936.pdf


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August 19, 2023
August 19, 2023