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J Biol Chem. 2003 Mar 7;278(10):8219-23. Epub 2003 Jan 3.

Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae.

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  • 1Russell Grimwade School of Biochemistry & Molecular Biology, University of Melbourne, Parkville 3010, Australia.


Tail-anchored proteins have an NH(2)-terminal cytosolic domain anchored to intracellular membranes by a single, COOH-terminal, transmembrane segment. Sequence analysis identified 55 tail-anchored proteins in Saccharomyces cerevisiae, with several novel proteins, including Prm3, which we find is required for karyogamy and is tail-anchored in the nuclear envelope. A total of six tail-anchored proteins are present in the mitochondrial outer membrane and have relatively hydrophilic transmembrane segments that serve as targeting signals. The rest, by far the majority, localize via a bipartite system of signals: uniformly hydrophobic tail anchors are first inserted into the endoplasmic reticulum, and additional segments within the cytosolic domain of each protein can dictate subsequent sorting to a precise destination within the cell.

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