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Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at contacts with forming autophagosomal membranes

Author

Listed:
  • Keisuke Mochida

    (School of Life Science and Technology, Tokyo Institute of Technology)

  • Akinori Yamasaki

    (Institute of Microbial Chemistry (BIKAKEN)
    Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology)

  • Kazuaki Matoba

    (Institute of Microbial Chemistry (BIKAKEN))

  • Hiromi Kirisako

    (School of Life Science and Technology, Tokyo Institute of Technology)

  • Nobuo N. Noda

    (Institute of Microbial Chemistry (BIKAKEN))

  • Hitoshi Nakatogawa

    (School of Life Science and Technology, Tokyo Institute of Technology)

Abstract

The endoplasmic reticulum (ER) is selectively degraded by autophagy (ER-phagy) through proteins called ER-phagy receptors. In Saccharomyces cerevisiae, Atg40 acts as an ER-phagy receptor to sequester ER fragments into autophagosomes by binding Atg8 on forming autophagosomal membranes. During ER-phagy, parts of the ER are morphologically rearranged, fragmented, and loaded into autophagosomes, but the mechanism remains poorly understood. Here we find that Atg40 molecules assemble in the ER membrane concurrently with autophagosome formation via multivalent interaction with Atg8. Atg8-mediated super-assembly of Atg40 generates highly-curved ER regions, depending on its reticulon-like domain, and supports packing of these regions into autophagosomes. Moreover, tight binding of Atg40 to Atg8 is achieved by a short helix C-terminal to the Atg8-family interacting motif, and this feature is also observed for mammalian ER-phagy receptors. Thus, this study significantly advances our understanding of the mechanisms of ER-phagy and also provides insights into organelle fragmentation in selective autophagy of other organelles.

Suggested Citation

  • Keisuke Mochida & Akinori Yamasaki & Kazuaki Matoba & Hiromi Kirisako & Nobuo N. Noda & Hitoshi Nakatogawa, 2020. "Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at contacts with forming autophagosomal membranes," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17163-y
    DOI: 10.1038/s41467-020-17163-y
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    Cited by:

    1. Taeko Sasaki & Yasuharu Kushida & Takuya Norizuki & Hidetaka Kosako & Ken Sato & Miyuki Sato, 2024. "ALLO-1- and IKKE-1-dependent positive feedback mechanism promotes the initiation of paternal mitochondrial autophagy," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Rayene Berkane & Hung Ho-Xuan & Marius Glogger & Pablo Sanz-Martinez & Lorène Brunello & Tristan Glaesner & Santosh Kumar Kuncha & Katharina Holzhüter & Sara Cano-Franco & Viviana Buonomo & Paloma Cab, 2023. "The function of ER-phagy receptors is regulated through phosphorylation-dependent ubiquitination pathways," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Ning Wang & Yoko Shibata & Joao A. Paulo & Steven P. Gygi & Tom A. Rapoport, 2023. "A conserved membrane curvature-generating protein is crucial for autophagosome formation in fission yeast," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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