| First Author | Chino H | Year | 2019 |
| Journal | Mol Cell | Volume | 74 |
| Issue | 5 | Pages | 909-921.e6 |
| PubMed ID | 31006538 | Mgi Jnum | J:278382 |
| Mgi Id | MGI:6323456 | Doi | 10.1016/j.molcel.2019.03.033 |
| Citation | Chino H, et al. (2019) Intrinsically Disordered Protein TEX264 Mediates ER-phagy. Mol Cell 74(5):909-921.e6 |
| abstractText | 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. |
