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CCPG1 recognizes endoplasmic reticulum luminal proteins for selective ER-phagy.
Ishii, Shunsuke; Chino, Haruka; Ode, Koji L; Kurikawa, Yoshitaka; Ueda, Hiroki R; Matsuura, Akira; Mizushima, Noboru; Itakura, Eisuke.
Afiliación
  • Ishii S; Department of Biology, Graduate School of Science and Engineering, Chiba University, Chiba 263-8522, Japan.
  • Chino H; Department of Biochemistry and Molecular Biology, Graduate School of Medicine, Tokyo 113-0033, Japan.
  • Ode KL; Department of Systems Pharmacology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan.
  • Kurikawa Y; Department of Biochemistry and Molecular Biology, Graduate School of Medicine, Tokyo 113-0033, Japan.
  • Ueda HR; Department of Systems Pharmacology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan.
  • Matsuura A; Laboratory for Synthetic Biology, RIKEN Center for Biosystems Dynamics Research, Osaka 565-0871, Japan.
  • Mizushima N; Department of Biology, Graduate School of Science, Chiba University, Chiba, 263-8522, Japan.
  • Itakura E; Department of Biochemistry and Molecular Biology, Graduate School of Medicine, Tokyo 113-0033, Japan.
Mol Biol Cell ; 34(4): ar29, 2023 04 01.
Article en En | MEDLINE | ID: mdl-36735498
The endoplasmic reticulum (ER) is a major cell compartment where protein synthesis, folding, and posttranslational modifications occur with assistance from a wide variety of chaperones and enzymes. Quality control systems selectively eliminate abnormal proteins that accumulate inside the ER due to cellular stresses. ER-phagy, that is, selective autophagy of the ER, is a mechanism that maintains or reestablishes cellular and ER-specific homeostasis through removal of abnormal proteins. However, how ER luminal proteins are recognized by the ER-phagy machinery remains unclear. Here, we applied the aggregation-prone protein, six-repeated islet amyloid polypeptide (6xIAPP), as a model ER-phagy substrate and found that cell cycle progression 1 (CCPG1), which is an ER-phagy receptor, efficiently mediates its degradation via ER-phagy. We also identified prolyl 3-hydroxylase family member 4 (P3H4) as an endogenous cargo of CCPG1-dependent ER-phagy. The ER luminal region of CCPG1 contains several highly conserved regions that we refer to as cargo-interacting regions (CIRs); these interact directly with specific luminal cargos for ER-phagy. Notably, 6xIAPP and P3H4 interact directly with different CIRs. These findings indicate that CCPG1 is a bispecific ER-phagy receptor for ER luminal proteins and the autophagosomal membrane that contributes to the efficient removal of aberrant ER-resident proteins through ER-phagy.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Autofagia / Estrés del Retículo Endoplásmico Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2023 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Autofagia / Estrés del Retículo Endoplásmico Tipo de estudio: Prognostic_studies Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2023 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos