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The N-Degron Pathway Mediates ER-phagy.

Chang Hoon Ji1, Hee Yeon Kim2, Ah Jung Heo1

  • 1Protein Metabolism Medical Research Center and Department of Biomedical Sciences, College of Medicine, Seoul National University, Seoul 110-799, Republic of Korea.

Molecular Cell
|August 4, 2019
PubMed
Summary
This summary is machine-generated.

The N-degron pathway drives endoplasmic reticulum (ER) turnover via ER-phagy. This process involves TRIM13, p62, and N-terminal arginine substrates, offering new therapeutic targets for ER protein quality control.

Keywords:
ER homeostasisER protein quality controlER stress responseER-phagyN-degron pathwayN-terminal arginylationTRIM13endoplasmic reticulump62ubiquitinationα1-antitrypsin deficiency

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) faces constant proteotoxic stress and damage, requiring efficient degradation mechanisms.
  • Autophagy, particularly ER-phagy, is crucial for maintaining ER homeostasis and protein quality control.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which the N-degron pathway mediates ER-phagy.
  • To identify key proteins and modifications involved in ER turnover.
  • To explore pharmaceutical strategies for enhancing ER protein quality control.

Main Methods:

  • Investigated the role of the E3 ligase TRIM13 (RFP2) in ER-phagy.
  • Examined the interaction between TRIM13, p62 (sequestosome-1), and arginylated substrates.
  • Utilized synthetic ligands targeting the p62 ZZ domain.

Main Results:

  • Demonstrated that K63-linked ubiquitination of TRIM13 initiates ER-phagy.
  • Showed that p62 oligomerization, triggered by N-terminal arginine (Nt-Arg) substrates, is essential for ER targeting.
  • Confirmed that TRIM13-p62 complexes mediate the degradation of ER compartments and luminal aggregates.
  • Developed synthetic ligands that enhance ER-phagy and alleviate ER stress.

Conclusions:

  • The N-degron pathway, through TRIM13 and p62, is a key regulator of ER-phagy.
  • Targeting the p62 ZZ domain with synthetic ligands offers a therapeutic approach to improve ER homeostasis and protein quality control.