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Curvature induction and membrane remodeling by FAM134B reticulon homology domain assist selective ER-phagy

Author

Listed:
  • Ramachandra M. Bhaskara

    (Max Planck Institute of Biophysics)

  • Paolo Grumati

    (Goethe University Frankfurt)

  • Javier Garcia-Pardo

    (Goethe University Frankfurt
    Division for Translational Medicine and Pharmacology)

  • Sissy Kalayil

    (Goethe University Frankfurt)

  • Adriana Covarrubias-Pinto

    (Goethe University Frankfurt)

  • Wenbo Chen

    (Goethe University Frankfurt
    Max Planck Institute of Biophysics)

  • Mikhail Kudryashev

    (Goethe University Frankfurt
    Max Planck Institute of Biophysics)

  • Ivan Dikic

    (Goethe University Frankfurt
    Goethe University Frankfurt)

  • Gerhard Hummer

    (Max Planck Institute of Biophysics
    Goethe University Frankfurt)

Abstract

FAM134B/RETREG1 is a selective ER-phagy receptor that regulates the size and shape of the endoplasmic reticulum. The structure of its reticulon-homology domain (RHD), an element shared with other ER-shaping proteins, and the mechanism of membrane shaping remain poorly understood. Using molecular modeling and molecular dynamics (MD) simulations, we assemble a structural model for the RHD of FAM134B. Through MD simulations of FAM134B in flat and curved membranes, we relate the dynamic RHD structure with its two wedge-shaped transmembrane helical hairpins and two amphipathic helices to FAM134B functions in membrane-curvature induction and curvature-mediated protein sorting. FAM134B clustering, as expected to occur in autophagic puncta, amplifies the membrane-shaping effects. Electron microscopy of in vitro liposome remodeling experiments support the membrane remodeling functions of the different RHD structural elements. Disruption of the RHD structure affects selective autophagy flux and leads to disease states.

Suggested Citation

  • Ramachandra M. Bhaskara & Paolo Grumati & Javier Garcia-Pardo & Sissy Kalayil & Adriana Covarrubias-Pinto & Wenbo Chen & Mikhail Kudryashev & Ivan Dikic & Gerhard Hummer, 2019. "Curvature induction and membrane remodeling by FAM134B reticulon homology domain assist selective ER-phagy," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10345-3
    DOI: 10.1038/s41467-019-10345-3
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    Cited by:

    1. Ewa Sitarska & Silvia Dias Almeida & Marianne Sandvold Beckwith & Julian Stopp & Jakub Czuchnowski & Marc Siggel & Rita Roessner & Aline Tschanz & Christer Ejsing & Yannick Schwab & Jan Kosinski & Mic, 2023. "Sensing their plasma membrane curvature allows migrating cells to circumvent obstacles," Nature Communications, Nature, vol. 14(1), pages 1-15, 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.

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