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  Doa10 is a membrane protein retrotranslocase in ER-associated protein degradation

Schmidt, C. C., Vasic, V., & Stein, A. (2020). Doa10 is a membrane protein retrotranslocase in ER-associated protein degradation. eLife, 9: e56945. doi:10.7554/eLife.56945.

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Schmidt, C. C.1, Author           
Vasic, V.1, Author           
Stein, A.1, Author           
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1Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_2149675              

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Free keywords: ERAD; protein quality control; protein translocation; ubiquitin proteasome system; membrane proteins; in vitro reconstitution; Research organism: S. cerevisiae
 Abstract: In endoplasmic reticulum-associated protein degradation (ERAD), membrane proteins are ubiquitinated, extracted from the membrane, and degraded by the proteasome. The cytosolic ATPase Cdc48 drives extraction by pulling on polyubiquitinated substrates. How hydrophobic transmembrane (TM) segments are moved from the phospholipid bilayer into cytosol, often together with hydrophilic and folded ER luminal protein parts, is not known. Using a reconstituted system with purified proteins from Saccharomyces cerevisiae, we show that the ubiquitin ligase Doa10 (Teb-4/MARCH6 in animals) is a retrotranslocase that facilitates membrane protein extraction. A substrate’s TM segment interacts with the membrane-embedded domain of Doa10 and then passively moves into the aqueous phase. Luminal substrate segments cross the membrane in an unfolded state. Their unfolding occurs on the luminal side of the membrane by cytoplasmic Cdc48 action. Our results reveal how a membrane-bound retrotranslocase cooperates with the Cdc48 ATPase in membrane protein extraction.

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Language(s): eng - English
 Dates: 2020-06-26
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.56945
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Title: eLife
Source Genre: Journal
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Pages: 31 Volume / Issue: 9 Sequence Number: e56945 Start / End Page: - Identifier: -