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Fine-tuning ER-phagy by post-translational modifications.
Eldeeb, Mohamed A; Zorca, Cornelia E; Ragheb, Mohamed A; Rashidi, Fatma B; Salah El-Din, Doaa S.
Afiliación
  • Eldeeb MA; McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
  • Zorca CE; McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
  • Ragheb MA; Chemistry Department (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt.
  • Rashidi FB; Chemistry Department (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt.
  • Salah El-Din DS; Chemistry Department (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt.
Bioessays ; 43(2): e2000212, 2021 02.
Article en En | MEDLINE | ID: mdl-33210303
Autophagy functions in both selective and non-selective ways to maintain cellular homeostasis. Endoplasmic reticulum autophagy (ER-phagy) is a subclass of autophagy responsible for the degradation of the endoplasmic reticulum through selective encapsulation into autophagosomes. ER-phagy occurs both under physiological conditions and in response to stress cues, and plays a crucial role in maintaining the homeostatic control of the organelle. Although specific receptors that target parts of the ER membrane, as well as, internal proteins for lysosomal degradation have been identified, the molecular regulation of ER-phagy has been elusive. Recent work has uncovered novel regulators of ER-phagy that involve post-translational modifications of ER-resident proteins and functional cross-talk with other cellular processes. Herein, we discuss how morphology affects the function of the peripheral ER, and how ER-phagy modulates the turnover of this organelle. We also address how ER-phagy is regulated at the molecular level, considering implications relevant to human diseases.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estrés del Retículo Endoplásmico / Proteínas de la Membrana Límite: Humans Idioma: En Revista: Bioessays Asunto de la revista: BIOLOGIA / BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estrés del Retículo Endoplásmico / Proteínas de la Membrana Límite: Humans Idioma: En Revista: Bioessays Asunto de la revista: BIOLOGIA / BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos