A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation

Author:

Cui Yixian1ORCID,Parashar Smriti1ORCID,Zahoor Muhammad2ORCID,Needham Patrick G.3ORCID,Mari Muriel4,Zhu Ming1,Chen Shuliang1ORCID,Ho Hsuan-Chung1ORCID,Reggiori Fulvio4,Farhan Hesso2,Brodsky Jeffrey L.3ORCID,Ferro-Novick Susan1ORCID

Affiliation:

1. Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, CA 92093, USA.

2. Institute of Basic Medical Sciences, Department of Molecular Medicine, University of Oslo, Sognsvannsveien 9, 0372 Oslo, Norway.

3. Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.

4. Department of Biomedical Sciences of Cells and Systems, University of Groningen Medical Center, Groningen, Netherlands.

Abstract

ER-phagy keeps cells healthy In eukaryotic cells, about one-third of all proteins are targeted to the endoplasmic reticulum (ER), which serves as a hub for secretory protein traffic and quality control. Cui et al. studied a protein known as Lst1 in yeast and SEC24C in mammalian cells that is involved in loading secretory cargo into vesicles that are delivered to the Golgi complex. In response to stress caused by starvation or misfolded aggregate-prone secretory proteins, Lst1 acted to promote an additional function—ER-phagy. Together with autophagy receptors on the ER, Lst1 targeted ER domains for degradation to avert protein aggregation, thus preserving cellular health. Science , this issue p. 53

Funder

National Institute of General Medical Sciences

National Institute of Diabetes and Digestive and Kidney Diseases

Marie Skłodowska-Curiee ITN

Marie Skłodowska-Curie Cofund

ALW Open Program

ZonMW VICI

ZonMW TOP

ALW Open Program grant

Norwegian Cancer Society

Norwegian Research Council

Ander Jahre Foundation

ALPHA-1 FOUNDATION

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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