Arginine Methylation Modulates Autophagic Degradation of PGL Granules in C. elegans

作者：Li, Sihui; Yang, Peiguo; Tian, E.; Zhang, Hong^*

来源：Molecular Cell, 2013, 52(3): 421-433.

DOI：10.1016/j.molcel.2013.09.014

• SELECTIVE AUTOPHAGY
• LINKS CARGO
• PROTEIN
• PHOSPHORYLATION
• ATG32
• MECHANISMS
• HUNTINGTIN
• COMPONENTS
• LESSONS
• ATG11

The selective degradation of intracellular components by autophagy involves sequential interactions of the cargo with a receptor, which also binds the autophagosonnal 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.

• 出版日期2013-11-7
• 单位北京生命科学研究所; 北京大学; 生物大分子国家重点实验室; 中国科学院