title: The nascent polypeptide-associated complex is essential for autophagic flux.
abstract: The ribosome-associated nascent polypeptide-associated complex (NAC) is involved in multiple cotranslational processes, including protein transport into the ER and mitochondria, and also acts as a chaperone to assist protein folding. Here we demonstrated that NAC is also essential for autophagic degradation of a variety of protein aggregates in C. elegans. Loss of function of NAC impairs lysosome function, resulting in accumulation of autophagic substrates in enlarged autolysosomes. Knockdown of mammalian NAC also causes accumulation of nondegradative autolysosomes. Our study revealed that NAC plays an evolutionarily conserved role in the autophagy pathway and thus in maintaining protein homeostasis under physiological conditions.
authors.affiliation: State Key Laboratory of Biomacromolecules; Institute of Biophysics; Chinese Academy of Sciences; Beijing, China.
authors.forename: Bin
authors.initials: B
authors.lastname: Guo
authors.affiliation: Key Laboratory of Medical Immunology; Ministry of Health; Peking University Health Science Center; Beijing, China; State Key Laboratory of Biomacromolecules; Institute of Biophysics; Chinese Academy of Sciences; Beijing, China.
authors.forename: Jie
authors.initials: J
authors.lastname: Huang
authors.affiliation: Institute of Neurology; Key Laboratory of Age-Associated Cardiac-Cerebral Vascular Disease of Guangdong Province; Affiliated Hospital of Guangdong Medical College; Zhanjiang, China.
authors.forename: Wenxian
authors.initials: W
authors.lastname: Wu
authors.affiliation: Institute of Neurology; Key Laboratory of Age-Associated Cardiac-Cerebral Vascular Disease of Guangdong Province; Affiliated Hospital of Guangdong Medical College; Zhanjiang, China.
authors.forename: Du
authors.initials: D
authors.lastname: Feng
authors.affiliation: National Institute of Biological Sciences; Beijing, China.
authors.forename: Xiaochen
authors.initials: X
authors.lastname: Wang
authors.affiliation: Key Laboratory of Medical Immunology; Ministry of Health; Peking University Health Science Center; Beijing, China.
authors.forename: Yingyu
authors.initials: Y
authors.lastname: Chen
authors.affiliation: State Key Laboratory of Biomacromolecules; Institute of Biophysics; Chinese Academy of Sciences; Beijing, China.
authors.forename: Hong
authors.initials: H
authors.lastname: Zhang
mesh_terms: D000818:Animals; D001343:Autophagy / Q000235:genetics; D017173:Caenorhabditis elegans / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D055785:Gene Knockdown Techniques; D017238:Genes, Helminth; D006367:HeLa Cells; D006801:Humans; D008247:Lysosomes / Q000378:metabolism; D008322:Mammals / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D021381:Protein Transport; D059748:Proteolysis; D034622:RNA Interference
chemical_list: D029742:Caenorhabditis elegans Proteins; D018832:Molecular Chaperones; C096099:nascent-polypeptide-associated complex
keywords: C. elegans; NAC; autophagy; lysosome