Tail-anchored and signal-anchored proteins utilize overlapping pathways during membrane insertion

ABELL, Benjamin, JUNG, Martin, OLIVER, Jason D., KNIGHT, Bruce C., TYEDMERS, Jens, ZIMMERMANN, Richard and HIGH, Stephen (2003). Tail-anchored and signal-anchored proteins utilize overlapping pathways during membrane insertion. Journal of Biological Chemistry, 278 (8), 5669-5678.

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Link to published version:: https://doi.org/10.1074/jbc.M209968200
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    Tail-anchored proteins are a distinct class of membrane proteins that are characterized by a C-terminal membrane insertion sequence and a capacity for post-translational integration. Although it is now clear that tail-anchored proteins are inserted into the membrane at the endoplasmic reticulum (ER), the molecular basis for their integration is poorly understood. We have used a cross-linking approach to identify ER components that may be involved in the membrane insertion of tail-anchored proteins. We find that several newly synthesized tail-anchored proteins are transiently associated with a defined subset of cellular components. Among these, we identify several ER proteins, including subunits of the Sec61 translocon, Sec62p, Sec63p, and the 25-kDa subunit of the signal peptidase complex. When we analyze the cotranslational membrane insertion of a comparable signal-anchored protein we find the nascent polypeptide associated with a similar set of ER components. We conclude that the pathways for the integration of tail-anchored and signal-anchored membrane proteins at the ER exhibit a substantial degree of overlap, and we propose that this reflects similarities between co- and post-translational membrane insertion.

    Item Type: Article
    Research Institute, Centre or Group - Does NOT include content added after October 2018: Biomedical Research Centre
    Identification Number: https://doi.org/10.1074/jbc.M209968200
    Page Range: 5669-5678
    Depositing User: Ann Betterton
    Date Deposited: 15 Feb 2008
    Last Modified: 18 Mar 2021 21:45
    URI: https://shura.shu.ac.uk/id/eprint/366

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