Journal
MOLECULAR CELL
Volume 74, Issue 5, Pages 909-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2019.03.033
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Funding
- Japan Society for the Promotion of Science [25111005, 17J05822]
- Exploratory Research for Advanced Technology (ERATO) grant from the Japan Science and Technology Agency (JST) [JPMJER1702]
- Grants-in-Aid for Scientific Research [17J05822] Funding Source: KAKEN
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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.
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