Intrinsically Disordered Protein TEX264 Mediates ER-phagy.
Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a ... receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy). TEX264 is an ER protein with a single transmembrane domain and a LIR motif. TEX264 interacts with LC3 and GABARAP family proteins more efficiently and is expressed more ubiquitously than previously known ER-phagy receptors. ER-phagy is profoundly blocked by deletion of TEX264 alone and almost completely by additional deletion of FAM134B and CCPG1. A long intrinsically disordered region of TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomal membranes independently of its amino acid sequence. These results suggest that TEX264 is a major ER-phagy receptor.
Mesh Terms:
Amino Acid Sequence, Autophagy, Autophagy-Related Proteins, Cell Cycle Proteins, Endoplasmic Reticulum, Endoplasmic Reticulum Stress, Humans, Intracellular Signaling Peptides and Proteins, Intrinsically Disordered Proteins, Membrane Proteins, Microtubule-Associated Proteins, Neoplasm Proteins, Proteolysis
Amino Acid Sequence, Autophagy, Autophagy-Related Proteins, Cell Cycle Proteins, Endoplasmic Reticulum, Endoplasmic Reticulum Stress, Humans, Intracellular Signaling Peptides and Proteins, Intrinsically Disordered Proteins, Membrane Proteins, Microtubule-Associated Proteins, Neoplasm Proteins, Proteolysis
Mol. Cell
Date: Dec. 06, 2018
PubMed ID: 31006538
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