Arginine methylation modulates autophagic degradation of PGL granules in C. elegans.
Mol Cell
; 52(3): 421-33, 2013 Nov 07.
Article
em En
| MEDLINE
| ID: mdl-24140420
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.
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Base de dados:
MEDLINE
Assunto principal:
Arginina
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Autofagia
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Proteínas de Ligação a RNA
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Proteínas de Caenorhabditis elegans
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Desenvolvimento Embrionário
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Proteólise
Limite:
Animals
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article