Involved in autophagy (PubMed:20550938, PubMed:24140420, PubMed:24374177). Thought to act as an adapter protein that brings PGL granules to autophagic structures containing lgg-1 (PubMed:20550938). Association with other adapters such as sepa-1 is required for the accumulation and degradation of germ cell specific P-granules by autophagy in somatic cells (PubMed:24140420, PubMed:28806108). This ensures exclusive localization of the P-granules in germ cells (PubMed:24140420, PubMed:28806108). May also play a role in the removal of sepa-1 from somatic cells (PubMed:28806108). Interacts with sepa-1 (PubMed:24140420, PubMed:28806108). Interacts (via the LIR motifs) with lgg-1 and lgg-2 (PubMed:26687600). Shows strong interaction with lgg-1 and weak interaction with lgg-2 (PubMed:26687600). Co-localizes with sepa-1 in cytoplasmic aggregates. Aggregates of epg-2 peak in abundance at the 100 cell stage then decrease until they are very few at the comma stage (PubMed:20550938, PubMed:28806108). Absent from the 200 stage onwards (PubMed:24140420, PubMed:28806108). The LIR motifs (LC3-interacting region) are required for its interaction with lgg-1 and lgg-2. No colocalization of P-granule components with lgg-1 (PubMed:20550938). Furthermore, there is an accumulation of pgl-3 positive P-granules in somatic cells of embryos (PubMed:28806108). RNAi-mediated knockdown results in increased lgg-2-positive autophagosomes following fertilization and at later embryonic stages (PubMed:24374177).