The expanding role of the ER translocon in membrane protein folding

William R. Skach

    Research output: Contribution to journalComment/debatepeer-review

    34 Scopus citations

    Abstract

    Eukaryotic polytopic membrane proteins are cotranslationally inserted into the ER membrane by a multisubunit protein-conducting channel called the Sec61 translocon. Although most major translocon components have been identified and reconstituted, their stoichiometry and functional organization remain unknown. This has led to speculative and sometimes conflicting models describing how multiple transmembrane (TM) segments might be oriented and integrated during nascent polytopic protein biogenesis. Kida et al. (see p. 1441 of this issue) shed new insight into this area by demonstrating that functional translocons exhibit a remarkable flexibility by simultaneously accommodating at least two hydrophilic translocating peptides that are separated by multiple hydrophobic TMs. These surprising findings support an expanded role for the translocon in membrane protein biogenesis and require reassessment of current views based on a single small functional pore.

    Original languageEnglish (US)
    Pages (from-to)1333-1335
    Number of pages3
    JournalJournal of Cell Biology
    Volume179
    Issue number7
    DOIs
    StatePublished - Dec 31 2007

    ASJC Scopus subject areas

    • Cell Biology

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