Journal
MOLECULAR CELL
Volume 58, Issue 2, Pages 269-283Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2015.02.018
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Funding
- NCI NIH HHS [P30 CA069533, P30CA069533] Funding Source: Medline
- NEI NIH HHS [P30 EY010572, P30EY010572] Funding Source: Medline
- NHLBI NIH HHS [T32 HL083808] Funding Source: Medline
- NIDDK NIH HHS [DK51818, R01 DK051818] Funding Source: Medline
- NIGMS NIH HHS [R01 GM053457, GM53457, F32 GM083568] Funding Source: Medline
- NIH HHS [S10OD012246, S10 OD012246] Funding Source: Medline
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The ER Sec61 translocon is a large macromolecular machine responsible for partitioning secretory and membrane polypeptides into the lumen, cytosol, and lipid bilayer. Because the Sec61 protein-conducting channel has been isolated in multiple membrane-derived complexes, we determined how the nascent polypeptide modulates translocon component associations during defined cotranslational translocation events. The model substrate preprolactin (pPL) was isolated principally with Sec61 alpha beta gamma upon membrane targeting, whereas higher-order complexes containing OST, TRAP, and TRAM were stabilized following substrate translocation. Blocking pPL translocation by passenger domain folding favored stabilization of an alternate complex that contained Sec61, Sec62, and Sec63. Moreover, Sec62/63 stabilization within the translocon occurred for native endogenous substrates, such as the prion protein, and correlated with a delay in translocation initiation. These data show that cotranslational translocon contacts are ultimately controlled by the engaged nascent chain and the resultant substrate-driven translocation events.
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