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Nat Cell Biol. 2016 Nov;18(11):1173-1184. doi: 10.1038/ncb3423. Epub 2016 Oct 17.

Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery.

Author information

1
Università della Svizzera italiana, CH-6900 Lugano, Switzerland.
2
Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland.
3
Graduate School for Cellular and Biomedical Sciences, University of Bern, CH-3000 Bern, Switzerland.
4
Department of Biology, Swiss Federal Institute of Technology, CH-8093 Zurich, Switzerland.
5
Experimental Imaging Center, San Raffaele Scientific Institute, I-20132 Milan, Italy.
6
Medical Biochemistry and Molecular Biology, Saarland University, D-66421 Homburg, Germany.
7
Department of Biology, Institute of Biochemistry, Swiss Federal Institute of Technology, CH-8093 Zurich, Switzerland.
8
Department of Chemistry, University of Zurich, CH-8057 Zurich, Switzerland.
9
Institute for Genetics, University of Cologne, D-50674 Cologne, Germany.
10
Center for Integrative Genomics, University of Lausanne, CH-1015 Lausanne, Switzerland.
11
Ecole Polytechnique Fédérale de Lausanne, School of Life Sciences, CH-1015 Lausanne, Switzerland.

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.

PMID:
27749824
DOI:
10.1038/ncb3423
[Indexed for MEDLINE]

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