Autophagy involves the enclosure of intracellular material within the autophagosome and subsequent delivery to the lysosome for degradation. Selective autophagy is achieved through receptors that bind simultaneously to cargoes to be degraded and the Atg8 protein, which associates with the autophagosome membrane. Efficient degradation of specific cargoes also requires scaffold proteins that link the receptor–cargo complex with multiple ATG proteins. Li et al. report that the arginine methyltransferase ectopic P granules-11 (EPG-11) is required for the selective degradation of the P granule components PGL-1 and PGL-3 during Caenorhabditis elegans embryogenesis. EPG-11 methylated arginine residues in PGL-1 and PGL-3, which was necessary for the association of PGL-1–PGL-3–SEPA-1 complexes (PGL granules, in which SEPA-1 is a receptor) with the scaffold protein EPG-2 and with LGG-1 (the C. elegans orthologue of Atg8). Arginine methylation thus regulates PGL degradation via selective autophagy.