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

Cui, Y., Parashar, S., Zahoor, M., Needham, P. G., Mari, M., Zhu, M., Chen, S., Ho, H-C., Reggiori, F., Farhan, H., Brodsky, J. L. & Ferro-Novick, S., 5-Jul-2019, In : Science. 365, 6448, p. 53-60 8 p.

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

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DOI

  • Yixian Cui
  • Smriti Parashar
  • Muhammad Zahoor
  • Patrick G Needham
  • Muriel Mari
  • Ming Zhu
  • Shuliang Chen
  • Hsuan-Chung Ho
  • Fulvio Reggiori
  • Hesso Farhan
  • Jeffrey L Brodsky
  • Susan Ferro-Novick

The COPII-cargo adaptor complex Lst1-Sec23 selectively sorts proteins into vesicles that bud from the endoplasmic reticulum (ER) and traffic to the Golgi. Improperly folded proteins are prevented from exiting the ER and are degraded. ER-phagy is an autophagic degradation pathway that uses ER-resident receptors. Working in yeast, we found an unexpected role for Lst1-Sec23 in ER-phagy that was independent from its function in secretion. Up-regulation of the stress-inducible ER-phagy receptor Atg40 induced the association of Lst1-Sec23 with Atg40 at distinct ER domains to package ER into autophagosomes. Lst1-mediated ER-phagy played a vital role in maintaining cellular homeostasis by preventing the accumulation of an aggregation-prone protein in the ER. Lst1 function appears to be conserved because its mammalian homolog, SEC24C, was also required for ER-phagy.

Original languageEnglish
Pages (from-to)53-60
Number of pages8
JournalScience
Volume365
Issue number6448
Publication statusPublished - 5-Jul-2019

    Keywords

  • UNFOLDED PROTEIN RESPONSE, SELECTIVE AUTOPHAGY, CARGO, YEAST, LUNAPARK, PATHWAYS, TURNOVER, TRIGGERS, REQUIRES, TEX264

ID: 89191404