The two autophagy receptors p62/SQSTM1 and NBR1 are evolutionary related and interact with each other via their PB1 domains.Unique for NBR1 is an amphipathic helix located adjacent to its C-terminal UBA domain that interacts directly with liposomes containing acidic phospholipids.Using these two domains, ectopically expressed NBR1 induces the formation of aggregates with contents very different from those formed by p62 alone.NBR1 aggregates mainly consist of clusters of 40-60 nm single membrane vesicles, but also larger structures including peroxisomes and late endosomes.The contents of the aggregates are degraded by autophagy in a process depending on the LIR motif of NBR1.In collaboration with the group of Peter Kim we have previously demonstrated that NBR1 overexpression induces pexophagy.NBR1 vesicle clusters co-localize strongly with important autophagy proteins including ATG16L1 and ATG12, but they also co-localize with clathrin.We have identified and characterized a clathrin box motif in NBR1 that is responsible for a direct interaction between NBR1 and clathrin heavy chain.Studies on the importance of this interaction in NBR1-mediated selective autophagy will be presented.