The expanding role of the ER translocon in membrane protein folding

William R. Skach

Research output: Contribution to journalComment/debate

33 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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