Related to Fig. 7 . RTN3L–SEC24C, CUL3^KLHL12 and PINK1 target ERAD resistant misfolded proteins for ER-phagy at LNPK-marked junctions. (A) Top, siCtrl and siDRP1-treated cells were blotted for the presence of DRP1. GAPDH was used as a loading control. Bottom, siCtrl and siDRP1-treated cells were transfected with Akita-sfGFP. Left, representative images with 10 × 10 µm insets used in the quantitation (right) of ER junctions at the cell periphery (see Materials and methods). (B) Percentage of cell with large Akita puncta/condensates (≥0.5 µm²) were quantified. Error bars in A and B represent SEM, n = 3 independent experiments. The results were quantified from 34 to 38 cells in A, and 73–103 cells in B. NS: not significant (P ≥ 0.05), Student’s unpaired t test. (C) An Akita puncta associates with RTN3L (left) and enlarges in the sheet-like domain of an LNPK-marked junction where the E3 ligase that ubiquitinates RTN3L, CUL3^KLHL12, is recruited (right). SEC24C–SEC23 and FIP200 are needed to retain Akita condensates in LC3-containing autophagic structures called ERPHS (right) that are delivered to lysosomes (right) during ER-phagy. The PINK1 kinase, DRP1, and other ER tubulating proteins regulate the formation of peripheral junctions where ERPHS are formed. Key: Ub, ubiquitinated RTN3L. Source data are available for this figure: SourceData FS13.