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Peer-reviewedCC BY-NC-ND 4.0Autophagy

Receptor–cargo coupling during ER-autophagy depends on coat proteins and ER membrane properties

  • Shuliang Chen1
  • Subhrajit Banerjee2
  • Peter Novick1
  • William A. Prinz2
  • Susan Ferro-Novick1
  1. 1Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla CA, USA
  2. 2Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA
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Abstract

Selective autophagy of the endoplasmic reticulum (reticulophagy) is driven by receptor-mediated ER remodeling. Reticulophagy receptors are essential for ER turnover. Productive cargo recognition during autophagosome-mediated reticulophagy depends on the interaction of the receptor with the COPII subunit Sfb3/Lst1 (SEC24C in mammals) as well as the phospholipid composition of the ER. We unexpectedly found that the conserved reticulophagy receptor Atg40 traffics to the vacuole/lysosome without cargo (ER membrane proteins) or Sfb3/Lst1 in neutral lipid-deficient mutant cells. Comprehensive lipidomic profiling of this lipid mutant revealed a shift in the phosphatidylethanolamine (PE)-to-phosphatidylcholine (PC) ratio, a compositional change predicted to alter biophysical properties of the ER, including membrane bendability. The discovery that membrane properties regulate receptor – cargo coupling efficiency at autophagic sites, as they do at secretory exit sites, extends current mechanistic models of reticulophagy and suggests membrane properties may also affect cargo selection on other types of selective autophagy pathways.

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Cite

BibTeXRIS
BibTeX
@article{chen2026receptorcargo,
  title = {{Receptor–cargo coupling during ER-autophagy depends on coat proteins and ER membrane properties}},
  author = {Shuliang Chen and Subhrajit Banerjee and Peter Novick and William A. Prinz and Susan Ferro-Novick},
  journal = {Autophagy},
  year = {2026},
  month = jul,
  doi = {10.1080/15548627.2026.2695313},
  url = {https://doi.org/10.1080/15548627.2026.2695313},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Receptor–cargo coupling during ER-autophagy depends on coat proteins and ER membrane properties
AU  - Shuliang Chen
AU  - Subhrajit Banerjee
AU  - Peter Novick
AU  - William A. Prinz
AU  - Susan Ferro-Novick
PY  - 2026
DA  - 2026/07/03
JO  - Autophagy
DO  - 10.1080/15548627.2026.2695313
UR  - https://doi.org/10.1080/15548627.2026.2695313
AB  - Selective autophagy of the endoplasmic reticulum (reticulophagy) is driven by receptor-mediated ER remodeling. Reticulophagy receptors are essential for ER turnover. Productive cargo recognition during autophagosome-mediated reticulophagy depends on the interaction of the receptor with the COPII subunit Sfb3/Lst1 (SEC24C in mammals) as well as the phospholipid composition of the ER. We unexpectedly found that the conserved reticulophagy receptor Atg40 traffics to the vacuole/lysosome without cargo (ER membrane proteins) or Sfb3/Lst1 in neutral lipid-deficient mutant cells. Comprehensive lipidomic profiling of this lipid mutant revealed a shift in the phosphatidylethanolamine (PE)-to-phosphatidylcholine (PC) ratio, a compositional change predicted to alter biophysical properties of the ER, including membrane bendability. The discovery that membrane properties regulate receptor – cargo coupling efficiency at autophagic sites, as they do at secretory exit sites, extends current mechanistic models of reticulophagy and suggests membrane properties may also affect cargo selection on other types of selective autophagy pathways.
SN  - 1554-8627
SN  - 1554-8635
ER  -