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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Intrinsically Disordered Protein TEX264 Mediates ER-phagy.

Haruka Chino1, Tomohisa Hatta2, Tohru Natsume2

  • 1Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan; Department of Respiratory Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.

Molecular Cell
|April 23, 2019
PubMed
Summary

Researchers identified TEX264 as a key receptor for endoplasmic reticulum-phagy (ER-phagy). This protein facilitates the selective degradation of the ER via autophagy, bridging ER and autophagosomal membranes.

Keywords:
ER-phagyintrinsically disordered regionorganellar contact siteselective autophagy

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Selective autophagy degrades specific cellular components.
  • LC3-interacting regions (LIRs) mediate substrate recognition by LC3 and GABARAP proteins on autophagosomes.
  • Endoplasmic reticulum-phagy (ER-phagy) targets the ER for autophagic degradation.

Purpose of the Study:

  • To identify novel receptors involved in selective autophagy, specifically ER-phagy.
  • To characterize the function and mechanism of identified ER-phagy receptors.

Main Methods:

  • Differential interactome screening using wild-type LC3B and a LIR-deficient mutant.
  • Identification and characterization of TEX264 as an ER-phagy receptor.
  • Genetic deletion studies (TEX264, FAM134B, CCPG1) to assess ER-phagy blockage.
  • Analysis of TEX264's structural requirements for ER-phagy function.

Main Results:

  • TEX264 was identified as a novel receptor for ER-phagy.
  • TEX264, an ER protein with a transmembrane domain and LIR motif, efficiently binds LC3/GABARAP proteins.
  • TEX264 exhibits broader expression than previously known ER-phagy receptors.
  • Deletion of TEX264 significantly impairs ER-phagy; combined deletion with FAM134B and CCPG1 almost completely blocks it.
  • An intrinsically disordered region of TEX264 is crucial for bridging ER and autophagosomal membranes.

Conclusions:

  • TEX264 is a major and essential receptor for ER-phagy.
  • The findings elucidate a key mechanism in selective ER degradation.
  • TEX264's unique structural features contribute to its vital role in ER homeostasis via autophagy.