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- W2940394744 endingPage "921.e6" @default.
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- W2940394744 abstract "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." @default.
- W2940394744 created "2019-04-25" @default.
- W2940394744 creator A5029906842 @default.
- W2940394744 creator A5038112377 @default.
- W2940394744 creator A5053187183 @default.
- W2940394744 creator A5063107400 @default.
- W2940394744 date "2019-06-01" @default.
- W2940394744 modified "2023-10-18" @default.
- W2940394744 title "Intrinsically Disordered Protein TEX264 Mediates ER-phagy" @default.
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- W2940394744 doi "https://doi.org/10.1016/j.molcel.2019.03.033" @default.
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