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Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Fumagalli F. , Noack J., Bergmann T.J., Cebollero E., Brambilla Pisoni G., Fasana E., Fregno I., Galli C., Loi M., Soldà T., D’Antuono R., Raimondi A., Jung M., Melnyk A., Schorr S., Schreiber A., Simonelli L., Varani L., Wilson-Zbinden C., Zerbe O., Hofmann K., Peter M., Quadroni M., Zimmermann R., Molinari M.,
Project ER-phagy mechanisms to maintain and restore endoplasmic reticulum homeostasis
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Original article (peer-reviewed)

Journal Nature Cell Biology
Volume (Issue) 18
Page(s) 1173 - 1184
Title of proceedings Nature Cell Biology
DOI 10.1038/ncb3423

Abstract

The endoplasmic reticulum (ER) is a site of protein biogenesis in eukaryotic cells. Perturbing ER homeostasis activates stress programs collectively called the unfolded protein response (UPR). The UPR enhances production of ER-resident chaperones and enzymes to reduce the burden of misfolded proteins. On resolution of ER stress, ill-defined, selective autophagic programs remove excess ER components. Here we identify Sec62, a constituent of the translocon complex regulating protein import in the mammalian ER, as an ER-resident autophagy receptor. Sec62 intervenes during recovery from ER stress to selectively deliver ER components to the autolysosomal system for clearance in a series of events that we name recovER-phagy. Sec62 contains a conserved LC3-interacting region in the C-terminal cytosolic domain that is required for its function in recovER-phagy, but is dispensable for its function in the protein translocation machinery. Our results identify Sec62 as a critical molecular component in maintenance and recovery of ER homeostasis.
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