Details

Autor(en) / Beteiligte

• Fumagalli, Fiorenza
• Noack, Julia
• Bergmann, Timothy J
• Cebollero, Eduardo
• Pisoni, Giorgia Brambilla
• Fasana, Elisa
• Fregno, Ilaria
• Galli, Carmela
• Loi, Marisa
• Soldà, Tatiana
• D'Antuono, Rocco
• Raimondi, Andrea
• Jung, Martin
• Melnyk, Armin
• Schorr, Stefan
• Schreiber, Anne
• Simonelli, Luca
• Varani, Luca
• Wilson-Zbinden, Caroline
• Zerbe, Oliver
• Hofmann, Kay
• Peter, Matthias
• Quadroni, Manfredo
• Zimmermann, Richard
• Molinari, Maurizio

Titel

Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery

Ist Teil von

• Nature cell biology, 2016-11, Vol.18 (11), p.1173-1184

Ort / Verlag

England

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.