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  Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo.

Rivera-Monroy, J., Musiol, L., Unthan-Fechner, K., Farkas, A., Clancy, A., Coy-Vergara, J., et al. (2016). Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo. Scientific Reports, 6: 39464. doi:10.1038/srep39464.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-3925-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-392B-1
Genre: Journal Article

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 Creators:
Rivera-Monroy, J., Author
Musiol, L., Author
Unthan-Fechner, K., Author
Farkas, A., Author
Clancy, A., Author
Coy-Vergara, J., Author
Weill, U., Author
Gockel, S., Author
Lin, S. Y., Author
Corey, D. P., Author
Kohl, T., Author
Strobel, P., Author
Schuldiner, M., Author
Schwappach, B.1, Author              
Vilardi, F., Author
Affiliations:
1Max Planck Fellow Blanche Schwappach, ou_1548137              

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 Abstract: Tail-anchored (TA) proteins are post-translationally inserted into membranes. The TRC40 pathway targets TA proteins to the endoplasmic reticulum via a receptor comprised of WRB and CAML. TRC40 pathway clients have been identified using in vitro assays, however, the relevance of the TRC40 pathway in vivo remains unknown. We followed the fate of TA proteins in two tissue-specific WRB knockout mouse models and found that their dependence on the TRC40 pathway in vitro did not predict their reaction to receptor depletion in vivo. The SNARE syntaxin 5 (Stx5) was extremely sensitive to disruption of the TRC40 pathway. Screening yeast TA proteins with mammalian homologues, we show that the particular sensitivity of Stx5 is conserved, possibly due to aggregation propensity of its cytoplasmic domain. We establish that Stx5 is an autophagy target that is inefficiently membrane-targeted by alternative pathways. Our results highlight an intimate relationship between the TRC40 pathway and cellular proteostasis.

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Language(s): eng - English
 Dates: 2016-12-21
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/srep39464
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Title: Scientific Reports
Source Genre: Journal
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Pages: 13 Volume / Issue: 6 Sequence Number: 39464 Start / End Page: - Identifier: -