title: Arginine methylation modulates autophagic degradation of PGL granules in C. elegans.
abstract: The selective degradation of intracellular components by autophagy involves sequential interactions of the cargo with a receptor, which also binds the autophagosomal protein Atg8 and a scaffold protein. Here, we demonstrated that mutations in C. elegans epg-11, which encodes an arginine methyltransferase homologous to PRMT1, cause the defective removal of PGL-1 and PGL-3 (cargo)-SEPA-1 (receptor) complexes, known as PGL granules, from somatic cells during embryogenesis. Autophagic degradation of the PGL granule scaffold protein EPG-2 and other protein aggregates was unaffected in epg-11/prmt-1 mutants. Loss of epg-11/prmt-1 activity impairs the association of PGL granules with EPG-2 and LGG-1 puncta. EPG-11/PRMT-1 directly methylates arginines in the RGG domains of PGL-1 and PGL-3. Autophagic removal of PGL proteins is impaired when the methylated arginines are mutated. Our study reveals that posttranslational arginine methylation regulates the association of the cargo-receptor complex with the scaffold protein, providing a mechanism for modulating degradation efficiency in selective autophagy.
authors.affiliation: College of Life Sciences, Peking University, Beijing 100875, China; State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; National Institute of Biological Sciences, Beijing 102206, China.
authors.forename: Sihui
authors.initials: S
authors.lastname: Li
authors.forename: Peiguo
authors.initials: P
authors.lastname: Yang
authors.forename: E
authors.initials: E
authors.lastname: Tian
authors.forename: Hong
authors.initials: H
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000235:genetics*; D001343:Autophagy / Q000235:genetics*; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000235:genetics* / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000378:metabolism; D047108:Embryonic Development; D008745:Methylation; D009154:Mutation; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism; D059748:Proteolysis; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism
chemical_list: D029742:Caenorhabditis elegans Proteins; C114543:PGL-1 protein, C elegans; C534959:PGL-3 protein, C elegans; D016601:RNA-Binding Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases